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Volumn 14, Issue 2, 1999, Pages 85-97

B-50/GAP-43 potentiates cytoskeletal reorganization in raft domains

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NEUROMODULIN;

EID: 0032854144     PISSN: 10447431     EISSN: None     Source Type: Journal    
DOI: 10.1006/mcne.1999.0775     Document Type: Article
Times cited : (32)

References (57)
  • 3
    • 0029113128 scopus 로고
    • The MARCKS family of protein kinase-C substrates
    • Aderem A. The MARCKS family of protein kinase-C substrates. Biochem. Soc. Trans. 23:1995;587-591.
    • (1995) Biochem. Soc. Trans. , vol.23 , pp. 587-591
    • Aderem, A.1
  • 4
    • 0028866034 scopus 로고
    • Overexpression of the neural growth-associated protein GAP-43 induces nerve sprouting in the adult nervous system of transgenic mice
    • Aigner L., Arber S., Kapfhammer J. P., Laux T., Schneider C., Botteri F., Brenner H. R., Caroni P. Overexpression of the neural growth-associated protein GAP-43 induces nerve sprouting in the adult nervous system of transgenic mice. Cell. 83:1995;269-278.
    • (1995) Cell , vol.83 , pp. 269-278
    • Aigner, L.1    Arber, S.2    Kapfhammer, J.P.3    Laux, T.4    Schneider, C.5    Botteri, F.6    Brenner, H.R.7    Caroni, P.8
  • 5
    • 0027360088 scopus 로고
    • Depletion of 43-kD growth-associated protein in primary sensory neurons leads to diminished formation and spreading of growth cones
    • Aigner L., Caroni P. Depletion of 43-kD growth-associated protein in primary sensory neurons leads to diminished formation and spreading of growth cones. J. Cell Biol. 123:1993;417-429.
    • (1993) J. Cell Biol. , vol.123 , pp. 417-429
    • Aigner, L.1    Caroni, P.2
  • 6
    • 0029086637 scopus 로고
    • Subcellular localization of moesin in dynamic filopodia, retraction fibers, and other structures involved in substrate exploration, attachment, and cell-cell contacts
    • Amieva M. R., Furthmayr H. Subcellular localization of moesin in dynamic filopodia, retraction fibers, and other structures involved in substrate exploration, attachment, and cell-cell contacts. Exp. Cell Res. 219:1995;180-196.
    • (1995) Exp. Cell Res. , vol.219 , pp. 180-196
    • Amieva, M.R.1    Furthmayr, H.2
  • 7
    • 0032561327 scopus 로고    scopus 로고
    • Association of GAP-43 with detergent-resistant membranes requires two palmitoylated cysteine residues
    • Arni S., Keilbaugh S. A., Ostermeyer A. G., Brown D. A. Association of GAP-43 with detergent-resistant membranes requires two palmitoylated cysteine residues. J. Biol. Chem. 273:1998;28478-28485.
    • (1998) J. Biol. Chem. , vol.273 , pp. 28478-28485
    • Arni, S.1    Keilbaugh, S.A.2    Ostermeyer, A.G.3    Brown, D.A.4
  • 8
    • 0026604761 scopus 로고
    • Internalization of glycosyl-phosphatidylinositol (GPI)-anchored lymphocyte proteins. II. GPI-anchored and transmembrane molecules internalize through distinct pathways
    • Bamezai A., Goldmacher V. S., Rock K. L. Internalization of glycosyl-phosphatidylinositol (GPI)-anchored lymphocyte proteins. II. GPI-anchored and transmembrane molecules internalize through distinct pathways. Eur. J. Immunol. 22:1992;15-21.
    • (1992) Eur. J. Immunol. , vol.22 , pp. 15-21
    • Bamezai, A.1    Goldmacher, V.S.2    Rock, K.L.3
  • 9
    • 0017350927 scopus 로고
    • Rat hippocampal neurons in dispersed cell culture
    • Banker G. A., Cowan W. M. Rat hippocampal neurons in dispersed cell culture. Brain Res. 126:1977;397-342.
    • (1977) Brain Res. , vol.126 , pp. 397-342
    • Banker, G.A.1    Cowan, W.M.2
  • 10
    • 0022470480 scopus 로고
    • Induction of membrane ruffling and fluid-phase pinocytosis in quiescent fibroblasts by ras proteins
    • Bar-Sagi D., Feramisco J. R. Induction of membrane ruffling and fluid-phase pinocytosis in quiescent fibroblasts by ras proteins. Science. 233:1986;1061-1068.
    • (1986) Science , vol.233 , pp. 1061-1068
    • Bar-Sagi, D.1    Feramisco, J.R.2
  • 11
    • 0021063404 scopus 로고
    • Increased transport of 44,000- To 49,000-dalton acidic proteins during regeneration of the goldfish optic nerve: A two-dimensional gel analysis
    • Benowitz L. I., Lewis E. R. Increased transport of 44,000- to 49,000-dalton acidic proteins during regeneration of the goldfish optic nerve: A two-dimensional gel analysis. J. Neurosci. 3:1983;2153-2163.
    • (1983) J. Neurosci. , vol.3 , pp. 2153-2163
    • Benowitz, L.I.1    Lewis, E.R.2
  • 12
    • 0026937122 scopus 로고
    • Glycosyl-phosphatidylinositol-anchored membrane proteins
    • Brown D., Waneck G. L. Glycosyl-phosphatidylinositol-anchored membrane proteins. J. Am. Soc. Nephrol. 3:1992;895-906.
    • (1992) J. Am. Soc. Nephrol. , vol.3 , pp. 895-906
    • Brown, D.1    Waneck, G.L.2
  • 13
    • 0026512314 scopus 로고
    • Sorting of GPI-anchored proteins to glycolipid-enriched membrane subdomains during transport to the apical cell surface
    • Brown D. A., 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
  • 14
    • 0025363426 scopus 로고
    • Localization of low molecular weight GTP binding proteins to exocytic and endocytic compartments
    • Chavrier P., Parton R. G., Hauri H. P., Simons K., Zerial M. Localization of low molecular weight GTP binding proteins to exocytic and endocytic compartments. Cell. 62:1990;317-329.
    • (1990) Cell , vol.62 , pp. 317-329
    • Chavrier, P.1    Parton, R.G.2    Hauri, H.P.3    Simons, K.4    Zerial, M.5
  • 15
    • 0026606451 scopus 로고
    • Suppression of kinesin expression in cultured hippocampal neurons using antisense oligonucleotides
    • Ferreira A., Niclas J., Vale R. D., Banker G., Kosik K. S. Suppression of kinesin expression in cultured hippocampal neurons using antisense oligonucleotides. J. Cell Biol. 117:1992;595-606.
    • (1992) J. Cell Biol. , vol.117 , pp. 595-606
    • Ferreira, A.1    Niclas, J.2    Vale, R.D.3    Banker, G.4    Kosik, K.S.5
  • 16
    • 0031952838 scopus 로고    scopus 로고
    • SNAP-25 palmitoylation and plasma membrane targeting require a functional secretory pathway
    • Gonzalo S., Linder M. E. SNAP-25 palmitoylation and plasma membrane targeting require a functional secretory pathway. Mol. Biol. Cell. 9:1998;585-597.
    • (1998) Mol. Biol. Cell , vol.9 , pp. 585-597
    • Gonzalo, S.1    Linder, M.E.2
  • 17
    • 0029918439 scopus 로고    scopus 로고
    • Mechanisms and molecules that control growth cone guidance
    • Goodman C. S. Mechanisms and molecules that control growth cone guidance. Annu. Rev. Neurosci. 19:1996;341-377.
    • (1996) Annu. Rev. Neurosci. , vol.19 , pp. 341-377
    • Goodman, C.S.1
  • 18
    • 0031750335 scopus 로고    scopus 로고
    • Lipid domain structure of the plasma membrane revealed by patching of membrane components
    • Harder T., Scheiffele P., Verkade P., Simons K. Lipid domain structure of the plasma membrane revealed by patching of membrane components. J. Cell Biol. 141:1998;929-942.
    • (1998) J. Cell Biol. , vol.141 , pp. 929-942
    • Harder, T.1    Scheiffele, P.2    Verkade, P.3    Simons, K.4
  • 19
    • 0030878573 scopus 로고    scopus 로고
    • Caveolae, DIGs, and the dynamics of sphingolipid-cholesterol microdomains
    • Harder T., Simons K. Caveolae, DIGs, and the dynamics of sphingolipid-cholesterol microdomains. Curr. Opin. Cell Biol. 9:1997;534-542.
    • (1997) Curr. Opin. Cell Biol. , vol.9 , pp. 534-542
    • Harder, T.1    Simons, K.2
  • 20
    • 0029795488 scopus 로고    scopus 로고
    • Regulation mechanism of ERM (ezrin/radixin/moesin) protein/plasma membrane association: Possible involvement of phosphatidylinositol turnover and Rho-dependent signaling pathway
    • Hirao M., Sato N., Kondo T., Yonemura S., Monden M., Sasaki T., Takai Y., Tsukita S. Regulation mechanism of ERM (ezrin/radixin/moesin) protein/plasma membrane association: Possible involvement of phosphatidylinositol turnover and Rho-dependent signaling pathway. J. Cell Biol. 135:1996;37-51.
    • (1996) J. Cell Biol. , vol.135 , pp. 37-51
    • Hirao, M.1    Sato, N.2    Kondo, T.3    Yonemura, S.4    Monden, M.5    Sasaki, T.6    Takai, Y.7    Tsukita, S.8
  • 21
    • 0029617651 scopus 로고
    • Directed expression of the growth-associated protein B-50/GAP-43 to olfactory neurons in transgenic mice results in changes in axon morphology and extraglomerular fiber growth
    • Holtmaat A. J. G. D., Dijkhuizen P. A., Oestreicher A. B., Romijn H. J., Van der Lugt N. M. T., Berns A., Margolis F. L., Gispen W. H., Verhaagen J. Directed expression of the growth-associated protein B-50/GAP-43 to olfactory neurons in transgenic mice results in changes in axon morphology and extraglomerular fiber growth. J. Neurosci. 15:1995;7953-7965.
    • (1995) J. Neurosci. , vol.15 , pp. 7953-7965
    • Holtmaat, A.J.G.D.1    Dijkhuizen, P.A.2    Oestreicher, A.B.3    Romijn, H.J.4    Van Der Lugt, N.M.T.5    Berns, A.6    Margolis, F.L.7    Gispen, W.H.8    Verhaagen, J.9
  • 24
    • 0026636973 scopus 로고
    • The low molecular weight guanosine triphosphate-binding protein Rab6p associates with distinct post-Golgi vesicles in Torpedo marmorata electrocytes
    • Jasmin B. J., Goud B., Camus G., Cartaud J. The low molecular weight guanosine triphosphate-binding protein Rab6p associates with distinct post-Golgi vesicles in Torpedo marmorata electrocytes. Neuroscience. 49:1992;849-855.
    • (1992) Neuroscience , vol.49 , pp. 849-855
    • Jasmin, B.J.1    Goud, B.2    Camus, G.3    Cartaud, J.4
  • 25
    • 0030979030 scopus 로고    scopus 로고
    • Association of Engrailed homeoproteins with vesicles presenting caveolae-like properties
    • Joliot A., Trembleau A., Raposo G., Calvet S., Volovitch M., Prochiantz A. Association of Engrailed homeoproteins with vesicles presenting caveolae-like properties. Development. 124:1997;1865-1875.
    • (1997) Development , vol.124 , pp. 1865-1875
    • Joliot, A.1    Trembleau, A.2    Raposo, G.3    Calvet, S.4    Volovitch, M.5    Prochiantz, A.6
  • 26
    • 0025320750 scopus 로고
    • The protein kinase C inhibitor H-7 activates human neutrophils: Effect on shape, actin polymerization, fluid pinocytosis and locomotion
    • Keller H. U., Niggli V., Zimmermann A., Portmann R. The protein kinase C inhibitor H-7 activates human neutrophils: Effect on shape, actin polymerization, fluid pinocytosis and locomotion. J. Cell Sci. 96:1990;99-106.
    • (1990) J. Cell Sci. , vol.96 , pp. 99-106
    • Keller, H.U.1    Niggli, V.2    Zimmermann, A.3    Portmann, R.4
  • 27
    • 0032584212 scopus 로고    scopus 로고
    • Neuronal polarity: Essential role of protein-lipid complexes in axonal sorting
    • Ledesma M. D., Simons K., Dotti C. G. Neuronal polarity: Essential role of protein-lipid complexes in axonal sorting. Proc. Natl. Acad. Sci. USA. 95:1998;3966-3971.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 3966-3971
    • Ledesma, M.D.1    Simons, K.2    Dotti, C.G.3
  • 28
    • 0027438823 scopus 로고
    • GAP 43-like immunoreactivity in normal adult rat sciatic nerve, spinal cord, and motoneurons: Axonal transport and effect of spinal cord transection
    • Li J. Y., Kling-Petersen A., Dahlstrom A. GAP 43-like immunoreactivity in normal adult rat sciatic nerve, spinal cord, and motoneurons: Axonal transport and effect of spinal cord transection. Neuroscience. 57:1993;759-776.
    • (1993) Neuroscience , vol.57 , pp. 759-776
    • Li, J.Y.1    Kling-Petersen, A.2    Dahlstrom, A.3
  • 29
    • 0027956969 scopus 로고
    • Intracellular sorting of neuromodulin (GAP-43) mutants modified in the membrane targeting domain
    • Liu Y., Fisher D. A., Storm D. R. Intracellular sorting of neuromodulin (GAP-43) mutants modified in the membrane targeting domain. J. Neurosci. 14:1994;5807-5817.
    • (1994) J. Neurosci. , vol.14 , pp. 5807-5817
    • Liu, Y.1    Fisher, D.A.2    Storm, D.R.3
  • 30
    • 0025148186 scopus 로고
    • Identification, sequencing and expression of an integral membrane protein of the trans-Golgi network (TGN38)
    • Luzio J. P., Brake B., Banting G., Howell K. E., Braghetta P., Stanley K. K. Identification, sequencing and expression of an integral membrane protein of the trans-Golgi network (TGN38). Biochem. J. 270:1990;97-102.
    • (1990) Biochem. J. , vol.270 , pp. 97-102
    • Luzio, J.P.1    Brake, B.2    Banting, G.3    Howell, K.E.4    Braghetta, P.5    Stanley, K.K.6
  • 31
    • 0030872949 scopus 로고    scopus 로고
    • Rho- And Rac-dependent assembly of focal adhesion complexes and actin filaments in permeabilized fibroblasts: An essential role for ezrin/radixin/moesin proteins
    • Mackay D. J. G., Esch F., Furthmayr H., Hall A. Rho- and Rac-dependent assembly of focal adhesion complexes and actin filaments in permeabilized fibroblasts: An essential role for ezrin/radixin/moesin proteins. J. Cell Biol. 138:1997;927-938.
    • (1997) J. Cell Biol. , vol.138 , pp. 927-938
    • Mackay, D.J.G.1    Esch, F.2    Furthmayr, H.3    Hall, A.4
  • 32
    • 0031029260 scopus 로고    scopus 로고
    • Identification of NAP-22 and GAP-43 (neuromodulin) as major protein components in a Triton insoluble low density fraction of rat brain
    • Maekawa S., Kumanogoh H., Funatsu N., Takei N., Inoue K., Endo Y., Hamada K., Sokawa Y. Identification of NAP-22 and GAP-43 (neuromodulin) as major protein components in a Triton insoluble low density fraction of rat brain. Biochim. Biophys. Acta. 1323:1997;1-5.
    • (1997) Biochim. Biophys. Acta , vol.1323 , pp. 1-5
    • Maekawa, S.1    Kumanogoh, H.2    Funatsu, N.3    Takei, N.4    Inoue, K.5    Endo, Y.6    Hamada, K.7    Sokawa, Y.8
  • 33
    • 0028987905 scopus 로고
    • Ezrin NH2-terminal domain inhibits the cell extension activity of the COOH-terminal domain
    • Martin M., Andreoli C., Sahuquet A., Montcourrier P., Algrain M., Mangeat P. Ezrin NH2-terminal domain inhibits the cell extension activity of the COOH-terminal domain. J. Cell Biol. 128:1995;1081-1093.
    • (1995) J. Cell Biol. , vol.128 , pp. 1081-1093
    • Martin, M.1    Andreoli, C.2    Sahuquet, A.3    Montcourrier, P.4    Algrain, M.5    Mangeat, P.6
  • 34
    • 0029044628 scopus 로고
    • Insolubility and redistribution of GPI-anchored proteins at the cell surface after detergent treatment
    • Mayor S., 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
  • 35
    • 0028000605 scopus 로고
    • Sequestration of GPI-anchored proteins in caveolae triggered by cross-linking
    • Mayor S., Rothberg K. G., Maxfield F. R. Sequestration of GPI-anchored proteins in caveolae triggered by cross-linking. Science. 264:1994;1948-1951.
    • (1994) Science , vol.264 , pp. 1948-1951
    • Mayor, S.1    Rothberg, K.G.2    Maxfield, F.R.3
  • 36
    • 0028880456 scopus 로고
    • Complexins: Cytosolic proteins that regulate SNAP receptor function
    • McMahon H. T., Missler M., Li C., Südhof T. C. Complexins: Cytosolic proteins that regulate SNAP receptor function. Cell. 83:1995;111-119.
    • (1995) Cell , vol.83 , pp. 111-119
    • McMahon, H.T.1    Missler, M.2    Li, C.3    Südhof, T.C.4
  • 37
    • 0029670673 scopus 로고    scopus 로고
    • Mutagenesis of Ser41 to Ala inhibits the association of GAP-43 with the membrane skeleton of GAP-43-deficient PC12B cells: Effects on cell adhesion and the composition of neurite cytoskeleton and membrane
    • Meiri K. F., Hammang J. P., Dent E. W., Baetge E. E. Mutagenesis of Ser41 to Ala inhibits the association of GAP-43 with the membrane skeleton of GAP-43-deficient PC12B cells: Effects on cell adhesion and the composition of neurite cytoskeleton and membrane. J. Neurobiol. 29:1996;213-232.
    • (1996) J. Neurobiol. , vol.29 , pp. 213-232
    • Meiri, K.F.1    Hammang, J.P.2    Dent, E.W.3    Baetge, E.E.4
  • 38
    • 0026684776 scopus 로고
    • Immunocytochemical detection of the growth associated protein B-50 by newly characterized monoclonal antibodies in human brain and muscle
    • Mercken M., Lubke U., Vandermeeren M., Gheuens J., Oestreicher A. B. Immunocytochemical detection of the growth associated protein B-50 by newly characterized monoclonal antibodies in human brain and muscle. J. Neurobiol. 23:1992;309-321.
    • (1992) J. Neurobiol. , vol.23 , pp. 309-321
    • Mercken, M.1    Lubke, U.2    Vandermeeren, M.3    Gheuens, J.4    Oestreicher, A.B.5
  • 39
    • 0029039937 scopus 로고
    • The dynamic role of palmitoylation in signal transduction
    • Milligan G., Parenti M., Magee A. I. The dynamic role of palmitoylation in signal transduction. Trends Biochem. Sci. 20:1995;181-187.
    • (1995) Trends Biochem. Sci. , vol.20 , pp. 181-187
    • Milligan, G.1    Parenti, M.2    Magee, A.I.3
  • 40
    • 0001704947 scopus 로고    scopus 로고
    • MARCKS regulates membrane ruffling and cell spreading
    • Myat M. M., Anderson S., Allen L. A. H., Aderem A. MARCKS regulates membrane ruffling and cell spreading. Curr. Biol. 7:1997;611-614.
    • (1997) Curr. Biol. , vol.7 , pp. 611-614
    • Myat, M.M.1    Anderson, S.2    Allen, L.A.H.3    Aderem, A.4
  • 41
    • 0027451304 scopus 로고
    • Spontaneous morphological changes by overexpression of the growth-associated protein B-50/GAP-43 in a PC12 cell line
    • Nielander H. B., French P., Oestreicher A. B., Gispen W. H., Schotman P. Spontaneous morphological changes by overexpression of the growth-associated protein B-50/GAP-43 in a PC12 cell line. Neurosci. Lett. 162:1993;46-50.
    • (1993) Neurosci. Lett. , vol.162 , pp. 46-50
    • Nielander, H.B.1    French, P.2    Oestreicher, A.B.3    Gispen, W.H.4    Schotman, P.5
  • 42
    • 0031452480 scopus 로고    scopus 로고
    • B-50, the growth associated protein-43: Modulation of cell morphology and communication in the nervous system
    • Oestreicher A. B., De Graan P. N. E., Gispen W. H., Verhaagen J., Schrama L. H. B-50, the growth associated protein-43: Modulation of cell morphology and communication in the nervous system. Prog. Neurobiol. 53:1997;627-686.
    • (1997) Prog. Neurobiol. , vol.53 , pp. 627-686
    • Oestreicher, A.B.1    De Graan, P.N.E.2    Gispen, W.H.3    Verhaagen, J.4    Schrama, L.H.5
  • 43
    • 0032493633 scopus 로고    scopus 로고
    • CD14-dependent endotoxin internalization via a macropinocytic pathway
    • Poussin C., Foti M., Carpentier J. L., Pugin J. CD14-dependent endotoxin internalization via a macropinocytic pathway. J. Biol. Chem. 273:1998;20285-20291.
    • (1998) J. Biol. Chem. , vol.273 , pp. 20285-20291
    • Poussin, C.1    Foti, M.2    Carpentier, J.L.3    Pugin, J.4
  • 44
    • 0026778133 scopus 로고
    • The small GTP-binding protein rho regulates the assembly of focal adhesions and actin stress fibers in response to growth factors
    • Ridley A. J., Hall A. The small GTP-binding protein rho regulates the assembly of focal adhesions and actin stress fibers in response to growth factors. Cell. 70:1992;389-399.
    • (1992) Cell , vol.70 , pp. 389-399
    • Ridley, A.J.1    Hall, A.2
  • 46
    • 0031964607 scopus 로고    scopus 로고
    • Cholesterol and sphingolipid enhance the Triton X-100 insolubility of glycosylphosphatidylinositol-anchored proteins by promoting the formation of detergent-insoluble ordered membrane domains
    • Schroeder R. J., Ahmed S. N., Zhu Y., London E., Brown D. A. Cholesterol and sphingolipid enhance the Triton X-100 insolubility of glycosylphosphatidylinositol-anchored proteins by promoting the formation of detergent-insoluble ordered membrane domains. J. Biol. Chem. 273:1998;1150-1157.
    • (1998) J. Biol. Chem. , vol.273 , pp. 1150-1157
    • Schroeder, R.J.1    Ahmed, S.N.2    Zhu, Y.3    London, E.4    Brown, D.A.5
  • 47
    • 0030949124 scopus 로고    scopus 로고
    • Functional rafts in cell membranes
    • Simons K., Ikonen E. Functional rafts in cell membranes. Nature. 387:1997;569-572.
    • (1997) Nature , vol.387 , pp. 569-572
    • Simons, K.1    Ikonen, E.2
  • 48
    • 0019828743 scopus 로고
    • Characteristics of growth-associated polypeptides in regenerating toad retinal ganglion cell axons
    • Skene J. H., Willard M. B. Characteristics of growth-associated polypeptides in regenerating toad retinal ganglion cell axons. J. Neurosci. 1:1981;419-426.
    • (1981) J. Neurosci. , vol.1 , pp. 419-426
    • Skene, J.H.1    Willard, M.B.2
  • 49
    • 0024576943 scopus 로고
    • Posttranslational membrane attachment and dynamic fatty acid acylation of a neuronal growth cone protein, GAP-43
    • Skene J. H. P., Virág I. Posttranslational membrane attachment and dynamic fatty acid acylation of a neuronal growth cone protein, GAP-43. J. Cell Biol. 108:1989;613-624.
    • (1989) J. Cell Biol. , vol.108 , pp. 613-624
    • Skene, J.H.P.1    Virág, I.2
  • 50
    • 0026448820 scopus 로고
    • Redistribution of B-50/growth-associated protein 43 during differentiation and maturation of rat hippocampal neurons in vitro
    • van Lookeren Campagne M., Dotti C. G., Verkleij A. J., Gispen W. H., Oestreicher A. B. Redistribution of B-50/growth-associated protein 43 during differentiation and maturation of rat hippocampal neurons in vitro. Neuroscience. 51:1992;601-619.
    • (1992) Neuroscience , vol.51 , pp. 601-619
    • Van Lookeren Campagne, M.1    Dotti, C.G.2    Verkleij, A.J.3    Gispen, W.H.4    Oestreicher, A.B.5
  • 51
    • 0028067830 scopus 로고
    • Expression of the growth-associated protein B-50/GAP43 via a defective herpes-simplex virus vector results in profound morphological changes in non-neuronal cells
    • Verhaagen J., Hermens W. T. J. M. C., Oestreicher A. B., Gispen W. H., Rabkin S. D., Pfaff D. W., Kaplitt M. G. Expression of the growth-associated protein B-50/GAP43 via a defective herpes-simplex virus vector results in profound morphological changes in non-neuronal cells. Mol. Brain Res. 26:1994;26-36.
    • (1994) Mol. Brain Res. , vol.26 , pp. 26-36
    • Verhaagen, J.1    Hermens, W.T.J.M.C.2    Oestreicher, A.B.3    Gispen, W.H.4    Rabkin, S.D.5    Pfaff, D.W.6    Kaplitt, M.G.7
  • 52
    • 0029961203 scopus 로고    scopus 로고
    • Ultrastructural evidence for the lack of co-transport of B-50/GAP-43 and calmodulin in myelinated axons of the regenerating rat sciatic nerve
    • Verkade P., Verkleij A. J., Gispen W. H., Oestreicher A. B. Ultrastructural evidence for the lack of co-transport of B-50/GAP-43 and calmodulin in myelinated axons of the regenerating rat sciatic nerve. J. Neurocytol. 25:1996;583-595.
    • (1996) J. Neurocytol. , vol.25 , pp. 583-595
    • Verkade, P.1    Verkleij, A.J.2    Gispen, W.H.3    Oestreicher, A.B.4
  • 53
    • 0019311309 scopus 로고
    • Subcellular compartmentalization of saccharide moieties in cultured neuronal and malignant cells
    • Virtanen I., Ekblom P., Laurila P. Subcellular compartmentalization of saccharide moieties in cultured neuronal and malignant cells. J. Cell Biol. 85:1980;429-434.
    • (1980) J. Cell Biol. , vol.85 , pp. 429-434
    • Virtanen, I.1    Ekblom, P.2    Laurila, P.3
  • 54
    • 0027439584 scopus 로고
    • Phosphorylation-site mutagenesis of the growth-associated protein GAP-43 modulates its effects on cell spreading and morphology
    • Widmer F., Caroni P. Phosphorylation-site mutagenesis of the growth-associated protein GAP-43 modulates its effects on cell spreading and morphology. J. Cell Biol. 120:1993;503-512.
    • (1993) J. Cell Biol. , vol.120 , pp. 503-512
    • Widmer, F.1    Caroni, P.2
  • 55
    • 0031563789 scopus 로고    scopus 로고
    • The motility-associated proteins GAP-43, MARCKS, and CAP-23 share unique targeting and surface activity-inducing properties
    • Wiederkehr A., Staple J., Caroni P. The motility-associated proteins GAP-43, MARCKS, and CAP-23 share unique targeting and surface activity-inducing properties. Exp. Cell Res. 236:1997;103-116.
    • (1997) Exp. Cell Res. , vol.236 , pp. 103-116
    • Wiederkehr, A.1    Staple, J.2    Caroni, P.3
  • 56
    • 0024390818 scopus 로고
    • The neuronal growth-associated protein GAP-43 induces filopodia in non-neuronal cells
    • Zuber M. X., Goodman D. W., Karns L. R., Fishman M. C. The neuronal growth-associated protein GAP-43 induces filopodia in non-neuronal cells. Science. 244:1989a;1193-1195.
    • (1989) Science , vol.244 , pp. 1193-1195
    • Zuber, M.X.1    Goodman, D.W.2    Karns, L.R.3    Fishman, M.C.4
  • 57
    • 0024956319 scopus 로고
    • A membrane-targeting signal in the amino terminus of the neuronal protein GAP-43
    • Zuber M. X., Strittmatter S. M., Fishman M. C. A membrane-targeting signal in the amino terminus of the neuronal protein GAP-43. Nature. 341:1989b;345-348.
    • (1989) Nature , vol.341 , pp. 345-348
    • Zuber, M.X.1    Strittmatter, S.M.2    Fishman, M.C.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.