메뉴 건너뛰기




Volumn , Issue 50TH ANN. SYMP., 1997, Pages 107-120

Molecular architecture of the specialized axonal membrane at the node of Ranvier

Author keywords

[No Author keywords available]

Indexed keywords

CONFERENCE PAPER; CYTOSKELETON; DROSOPHILA; MYELINATION; NERVE CONDUCTION; NERVE FIBER MEMBRANE; NERVE POTENTIAL; NONHUMAN; OLIGODENDROGLIA; ANIMAL; CELL MEMBRANE; CHEMISTRY; NERVE FIBER; RANVIER NODE; REVIEW; ULTRASTRUCTURE;

EID: 0030914810     PISSN: 00221295     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Conference Paper
Times cited : (26)

References (75)
  • 1
    • 0022349766 scopus 로고
    • Localization of sodium/potassium adenosine triphosphatase in multiple cell types of the murine nervous system with antibodies raised against the enzyme from kidney
    • Ariyasu, R.G., J.A. Nichol, and M.H. Ellisman. 1985. Localization of sodium/potassium adenosine triphosphatase in multiple cell types of the murine nervous system with antibodies raised against the enzyme from kidney. J. Neurosci. 5:2581-2596.
    • (1985) J. Neurosci. , vol.5 , pp. 2581-2596
    • Ariyasu, R.G.1    Nichol, J.A.2    Ellisman, M.H.3
  • 2
    • 0019824794 scopus 로고
    • Erythrocyte ankyrin: Immunoreactive analogues are associated with mitotic structures in cultured cells and with microtubules in brain
    • Bennett, V., and J. Davis. 1981. Erythrocyte ankyrin: immunoreactive analogues are associated with mitotic structures in cultured cells and with microtubules in brain. Proc. Natl. Acad. Sci. USA. 78:7550-7554.
    • (1981) Proc. Natl. Acad. Sci. USA , vol.78 , pp. 7550-7554
    • Bennett, V.1    Davis, J.2
  • 3
    • 0027333413 scopus 로고
    • The spectrin-based membrane skeleton and micron-scale organization of the plasma membrane
    • Bennett, V., and D.M. Gilligan. 1993. The spectrin-based membrane skeleton and micron-scale organization of the plasma membrane. Annu. Rev. Cell Biol. 9:27-66.
    • (1993) Annu. Rev. Cell Biol. , vol.9 , pp. 27-66
    • Bennett, V.1    Gilligan, D.M.2
  • 4
    • 0027155208 scopus 로고
    • Complex patterns of sequence variation and multiple 5′ and 3′ ends are found among transcripts of the erythroid ankyrin gene
    • Birkenmeier, C.S., R.A. White, L.L. Peters, E.J. Hall, S.E. Lux, and J.E. Barker. 1993. Complex patterns of sequence variation and multiple 5′ and 3′ ends are found among transcripts of the erythroid ankyrin gene. J. Biol. Chem. 268:9533-9540.
    • (1993) J. Biol. Chem. , vol.268 , pp. 9533-9540
    • Birkenmeier, C.S.1    White, R.A.2    Peters, L.L.3    Hall, E.J.4    Lux, S.E.5    Barker, J.E.6
  • 5
    • 0001795782 scopus 로고
    • Morphology of normal peripheral axons
    • G.S. Waxman, J.D. Kocsis, and P.K. Stys, editors. Oxford University Press, New York/Oxford
    • Berthold, C.H., and M. Rydmark. 1995. Morphology of normal peripheral axons. In The Axon, G.S. Waxman, J.D. Kocsis, and P.K. Stys, editors. Oxford University Press, New York/Oxford. 13-48.
    • (1995) The Axon , pp. 13-48
    • Berthold, C.H.1    Rydmark, M.2
  • 6
    • 0022365608 scopus 로고
    • The distribution of tau in the mammalian central nervous system
    • Binder, L.I., A. Frankfurter, and L.I. Rebhun. 1985. The distribution of tau in the mammalian central nervous system. J. Cell Biol. 101:1371-1378.
    • (1985) J. Cell Biol. , vol.101 , pp. 1371-1378
    • Binder, L.I.1    Frankfurter, A.2    Rebhun, L.I.3
  • 7
    • 0010570991 scopus 로고
    • The oligodendrocyte, the perinodal astrocyte, and the central node of Ranvier
    • G.S. Waxman, J.D. Kocsis, and P.K. Stys, editors. Oxford University Press, New York/Oxford
    • Black, J.A., H. Sontheimer, Y. Oh, and S.G. Waxman. 1995. The oligodendrocyte, the perinodal astrocyte, and the central node of Ranvier. In The Axon. G.S. Waxman, J.D. Kocsis, and P.K. Stys, editors. Oxford University Press, New York/Oxford. 116-143.
    • (1995) The Axon , pp. 116-143
    • Black, J.A.1    Sontheimer, H.2    Oh, Y.3    Waxman, S.G.4
  • 8
    • 0024256419 scopus 로고
    • The perinodal astrocyte
    • Black, J.A., and S. Waxman. 1988. The perinodal astrocyte. Glia. 1:1169-1183.
    • (1988) Glia , vol.1 , pp. 1169-1183
    • Black, J.A.1    Waxman, S.2
  • 9
    • 0027333330 scopus 로고
    • Hundreds of ankyrin-like repeats in functionally diverse proteins: Mobile modules that cross phyla horizontally?
    • Bork, P. 1993. Hundreds of ankyrin-like repeats in functionally diverse proteins: mobile modules that cross phyla horizontally? Proteins. 17:363-374.
    • (1993) Proteins , vol.17 , pp. 363-374
    • Bork, P.1
  • 10
    • 0023082941 scopus 로고
    • Tissue culture studies of interactions between axons and myelinating cells of the central and peripheral nervous system
    • Bunge, R.P., and P.M. Wood. 1987. Tissue culture studies of interactions between axons and myelinating cells of the central and peripheral nervous system. Prog. Brain Res. 71:43-152.
    • (1987) Prog. Brain Res. , vol.71 , pp. 43-152
    • Bunge, R.P.1    Wood, P.M.2
  • 11
    • 0029026638 scopus 로고
    • Structure and function of voltage-gated ion channels
    • Catterall, W.A. 1995. Structure and function of voltage-gated ion channels. Annu. Rev. Biochem. 64:493-531.
    • (1995) Annu. Rev. Biochem. , vol.64 , pp. 493-531
    • Catterall, W.A.1
  • 12
    • 0027729564 scopus 로고
    • B: Structure of the major developmentally regulated domain and selective localization in unmyelinated axons
    • B: structure of the major developmentally regulated domain and selective localization in unmyelinated axons. J. Cell Biol. 123:1463-1473.
    • (1993) J. Cell Biol. , vol.123 , pp. 1463-1473
    • Chan, W.1    Kordeli, E.2    Bennett, V.3
  • 13
    • 0029066697 scopus 로고
    • Contenders in Fas/TNF death signaling
    • Cleveland, J.L., and J.N. Ihle. 1995. Contenders in Fas/TNF death signaling. Cell. 81:479-482.
    • (1995) Cell , vol.81 , pp. 479-482
    • Cleveland, J.L.1    Ihle, J.N.2
  • 14
    • 0026722207 scopus 로고
    • Ankyrin regulation: An alternatively spliced segment of the regulatory domain functions as an intramolecular modulator
    • Davis, L.H., J.Q. Davis, and V. Bennett. 1992. Ankyrin regulation: an alternatively spliced segment of the regulatory domain functions as an intramolecular modulator. J. Biol. Chem. 267:18966-18972.
    • (1992) J. Biol. Chem. , vol.267 , pp. 18966-18972
    • Davis, L.H.1    Davis, J.Q.2    Bennett, V.3
  • 15
    • 0027999616 scopus 로고
    • Ankyrin-binding activity shared by the neurofascin/L1/NrCam family of nervous system cell adhesion molecules
    • Davis, J., and V. Bennett. 1994. Ankyrin-binding activity shared by the neurofascin/L1/NrCam family of nervous system cell adhesion molecules. J. Biol. Chem. 269:27163-27166.
    • (1994) J. Biol. Chem. , vol.269 , pp. 27163-27166
    • Davis, J.1    Bennett, V.2
  • 16
    • 0030443956 scopus 로고    scopus 로고
    • Molecular composition of the node of Ranvier: Identification of ankyrin-binding cell adhesion molecules neurofascin (mucin+/third FNIII domain-) and NrCAm at nodal axon segments
    • In press
    • Davis, J., S. Lambert, and V. Bennett. 1996. Molecular composition of the node of Ranvier: identification of ankyrin-binding cell adhesion molecules neurofascin (mucin+/third FNIII domain-) and NrCAm at nodal axon segments. J. Cell Biol. In press.
    • (1996) J. Cell Biol.
    • Davis, J.1    Lambert, S.2    Bennett, V.3
  • 17
    • 0027532185 scopus 로고
    • Ankyrin-binding proteins related to nervous system cell adhesion molecules: Candidates to provide transmembrane and intercellular connections in adult brain
    • Davis, J.Q., T. McLaughlin, and V. Bennett. 1993. Ankyrin-binding proteins related to nervous system cell adhesion molecules: candidates to provide transmembrane and intercellular connections in adult brain. J. Cell Biol. 232:121-133.
    • (1993) J. Cell Biol. , vol.232 , pp. 121-133
    • Davis, J.Q.1    McLaughlin, T.2    Bennett, V.3
  • 18
    • 0029898290 scopus 로고    scopus 로고
    • Identification of a small cytoplasmic ankyrin (AnkG119) in the kidney and muscle that binds beta spectrin and associates with the Golgi apparatus
    • Deverajan, P., P. Stabach, A.S. Mann, T. Ardito, M. Kashgarian, and J. Morrow. 1996. Identification of a small cytoplasmic ankyrin (AnkG119) in the kidney and muscle that binds beta spectrin and associates with the Golgi apparatus. J. Cell Biol. 133:819-830.
    • (1996) J. Cell Biol. , vol.133 , pp. 819-830
    • Deverajan, P.1    Stabach, P.2    Mann, A.S.3    Ardito, T.4    Kashgarian, M.5    Morrow, J.6
  • 19
    • 0026580004 scopus 로고
    • Local modulation of neurofilament phosphorylation, axonal caliber, and slow axonal transport by myelinating Schwann cells
    • deWaegh, S., V.M.-Y. Lee, and S.T. Brady. 1992. Local modulation of neurofilament phosphorylation, axonal caliber, and slow axonal transport by myelinating Schwann cells. Cell. 68:451-463.
    • (1992) Cell , vol.68 , pp. 451-463
    • Dewaegh, S.1    Lee, V.M.-Y.2    Brady, S.T.3
  • 21
    • 0028173073 scopus 로고
    • Ankyrin and beta-spectrin accumulate independently of alpha-spectrin in Drosophila
    • Dubreuil, R., and J. Yu. 1994. Ankyrin and beta-spectrin accumulate independently of alpha-spectrin in Drosophila. Proc. Natl. Acad. Sci. USA. 91:10285-10289.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 10285-10289
    • Dubreuil, R.1    Yu, J.2
  • 22
    • 0029899939 scopus 로고    scopus 로고
    • Neuroglian-mediated cell adhesion induces assembly of the membrane skeleton at cell contact sites
    • Dubreuil, R.R., R. MacVicar, S. Dissanayake, C. Liu, D. Homer, and M. Hortsch. 1996. Neuroglian-mediated cell adhesion induces assembly of the membrane skeleton at cell contact sites. J. Cell Biol. 133:647-655.
    • (1996) J. Cell Biol. , vol.133 , pp. 647-655
    • Dubreuil, R.R.1    MacVicar, R.2    Dissanayake, S.3    Liu, C.4    Homer, D.5    Hortsch, M.6
  • 25
    • 0028273033 scopus 로고
    • TAG-1 can mediate homophilic binding but neurite outgrowth on TAG-1 requires an L1-like molecule and betal integrins
    • Felsenfeld, D., M. Hynes, K. Skoler, A. Furley, and T.M. Jessel. 1994. TAG-1 can mediate homophilic binding but neurite outgrowth on TAG-1 requires an L1-like molecule and betal integrins. Neuron. 12:675-690.
    • (1994) Neuron , vol.12 , pp. 675-690
    • Felsenfeld, D.1    Hynes, M.2    Skoler, K.3    Furley, A.4    Jessel, T.M.5
  • 26
    • 0024708031 scopus 로고
    • Membrane proteins in the neuromuscular junction. Distribution of Na channels and ankyrin is complementary to acetylcholine receptors and the 43-kD protein
    • Flucher, B., and M. Daniels. 1989. Membrane proteins in the neuromuscular junction. Distribution of Na channels and ankyrin is complementary to acetylcholine receptors and the 43-kD protein. Neuron. 3:163-175.
    • (1989) Neuron , vol.3 , pp. 163-175
    • Flucher, B.1    Daniels, M.2
  • 27
    • 85012338162 scopus 로고
    • The binding of vimentin to human erythrocyte membranes: A model system for the study of intermediate filament-membrane interactions
    • Georgatos, S., and V. Marchesi. 1985. The binding of vimentin to human erythrocyte membranes: a model system for the study of intermediate filament-membrane interactions. J. Cell Biol. 100:1955-1961.
    • (1985) J. Cell Biol. , vol.100 , pp. 1955-1961
    • Georgatos, S.1    Marchesi, V.2
  • 28
    • 0024227007 scopus 로고
    • Development of neuronal polarity: GAP43 distinguishes axonal from dendritic growth cones
    • Goslin, K., J. Schreyer, P. Skene, and G. Banker. 1988. Development of neuronal polarity: GAP43 distinguishes axonal from dendritic growth cones. Nature. 336:672-674.
    • (1988) Nature , vol.336 , pp. 672-674
    • Goslin, K.1    Schreyer, J.2    Skene, P.3    Banker, G.4
  • 30
    • 0026235917 scopus 로고
    • Cell adhesion molecules and their subgroups in the nervous system
    • Grumet, M. 1991. Cell adhesion molecules and their subgroups in the nervous system. Curr. Opin. Neurobiol. 1:370-376.
    • (1991) Curr. Opin. Neurobiol. , vol.1 , pp. 370-376
    • Grumet, M.1
  • 31
    • 0023196746 scopus 로고
    • Regulatory domains of erythrocyte ankyrin
    • Hall, T.G., and V. Bennett. 1987. Regulatory domains of erythrocyte ankyrin. J. Biol. Chem. 262:10537-10545.
    • (1987) J. Biol. Chem. , vol.262 , pp. 10537-10545
    • Hall, T.G.1    Bennett, V.2
  • 32
    • 0026795976 scopus 로고
    • Glycosylation of nuclear and cytoplasmic fractions
    • Haltiwanger, R.S., M. Blomberg, and G.W. Hart. 1992. Glycosylation of nuclear and cytoplasmic fractions. J. Biol. Chem. 267:9005-9013.
    • (1992) J. Biol. Chem. , vol.267 , pp. 9005-9013
    • Haltiwanger, R.S.1    Blomberg, M.2    Hart, G.W.3
  • 33
    • 0025836732 scopus 로고
    • Cell and substrate adhesion molecules
    • Hortsch, M., and C. Goodman. 1991. Cell and substrate adhesion molecules. Annu. Rev. Cell Biol. 7:505-557.
    • (1991) Annu. Rev. Cell Biol. , vol.7 , pp. 505-557
    • Hortsch, M.1    Goodman, C.2
  • 34
    • 0025807797 scopus 로고
    • Three-dimensional fine structure of cytoskeletal-membrane interactions at nodes of Ranvier
    • Ichimura, T., and M.H. Ellisman. 1991. Three-dimensional fine structure of cytoskeletal-membrane interactions at nodes of Ranvier. J. Neurocytol. 20:667-681.
    • (1991) J. Neurocytol. , vol.20 , pp. 667-681
    • Ichimura, T.1    Ellisman, M.H.2
  • 35
    • 0028347820 scopus 로고
    • Impaired neurite outgrowth of srcminus cerebellar neurons on the cell adhesion molecule L1
    • Ignelzi, M., D. Miller, P. Soriano, and P.F. Maness. 1994. Impaired neurite outgrowth of srcminus cerebellar neurons on the cell adhesion molecule L1. Neuron. 12:873-884.
    • (1994) Neuron , vol.12 , pp. 873-884
    • Ignelzi, M.1    Miller, D.2    Soriano, P.3    Maness, P.F.4
  • 36
    • 0028972374 scopus 로고
    • Structure and function of the beta-2 subunit of brain sodium channels, a transmembrane glycoprotein with a CAM motif
    • Isom, L.L., D.S. Ragsdale, K. DeJongh, R.E. Westenboek, B.F. Reber, T. Scheuer, and W.A. Catterall. 1995. Structure and function of the beta-2 subunit of brain sodium channels, a transmembrane glycoprotein with a CAM motif. Cell. 83:433-442.
    • (1995) Cell , vol.83 , pp. 433-442
    • Isom, L.L.1    Ragsdale, D.S.2    Dejongh, K.3    Westenboek, R.E.4    Reber, B.F.5    Scheuer, T.6    Catterall, W.A.7
  • 37
    • 0029591842 scopus 로고
    • Identification of a binding motif for ankyrin on the a-subunit of Na,K-ATPase
    • Jordon, C., B. Puschel, R. Koob, and D. Drenckhahn. 1995. Identification of a binding motif for ankyrin on the a-subunit of Na,K-ATPase. J. Biol. Chem. 270:29971-29975.
    • (1995) J. Biol. Chem. , vol.270 , pp. 29971-29975
    • Jordon, C.1    Puschel, B.2    Koob, R.3    Drenckhahn, D.4
  • 38
    • 0021916280 scopus 로고
    • A regional analysis of alpha-spectrin in the isolated Mauthner neuron and in isolated axons of the goldfish and rabbit
    • Koenig, E., and E. Repasky. 1985. A regional analysis of alpha-spectrin in the isolated Mauthner neuron and in isolated axons of the goldfish and rabbit. J. Neurosci. 5:705-714.
    • (1985) J. Neurosci. , vol.5 , pp. 705-714
    • Koenig, E.1    Repasky, E.2
  • 39
    • 0026077783 scopus 로고
    • Distinct ankyrin isoforms at neuron cell bodies and nodes of Ranvier resolved using erythrocyte ankyrin-deficient mice
    • Kordeli, E., and V. Bennett. 1991. Distinct ankyrin isoforms at neuron cell bodies and nodes of Ranvier resolved using erythrocyte ankyrin-deficient mice. J. Cell Biol. 114:1243-1259.
    • (1991) J. Cell Biol. , vol.114 , pp. 1243-1259
    • Kordeli, E.1    Bennett, V.2
  • 40
    • 0025231649 scopus 로고
    • An isoform of ankyrin is localized at nodes of Ranvier in myelinated axons of central and peripheral nerves
    • Kordeli, E., J. Davis, B. Trapp, and V. Bennett. 1990. An isoform of ankyrin is localized at nodes of Ranvier in myelinated axons of central and peripheral nerves. J. Cell Biol. 110:1341-1352.
    • (1990) J. Cell Biol. , vol.110 , pp. 1341-1352
    • Kordeli, E.1    Davis, J.2    Trapp, B.3    Bennett, V.4
  • 41
    • 0028985712 scopus 로고
    • G: A new ankyrin gene with neural-specific isoforms localized at the axonal initial segment and node of Ranvier
    • G: a new ankyrin gene with neural-specific isoforms localized at the axonal initial segment and node of Ranvier. J. Biol. Chem. 270:2352-2359.
    • (1995) J. Biol. Chem. , vol.270 , pp. 2352-2359
    • Kordeli, E.1    Lambert, S.2    Bennett, V.3
  • 42
    • 0029558546 scopus 로고
    • B, is targeted to axons of rat cerebellar neurons
    • B, is targeted to axons of rat cerebellar neurons. J. Cell Biol. 131:1821-1830.
    • (1995) J. Cell Biol. , vol.131 , pp. 1821-1830
    • Kunimoto, M.1
  • 43
    • 0025840276 scopus 로고
    • A new 440-kDa isoform is the major ankyrin in neonatal rat brain
    • Kunimoto, M., E. Otto, and V. Bennett. 1991. A new 440-kDa isoform is the major ankyrin in neonatal rat brain. J. Cell Biol. 115:1319-1331.
    • (1991) J. Cell Biol. , vol.115 , pp. 1319-1331
    • Kunimoto, M.1    Otto, E.2    Bennett, V.3
  • 44
    • 0027393661 scopus 로고
    • From anemia to cerebellar dysfunction. A review of the ankyrin gene family
    • Lambert, S., and V. Bennett. 1993a. From anemia to cerebellar dysfunction. A review of the ankyrin gene family. Eur. J. Biochem. 211:1-6.
    • (1993) Eur. J. Biochem. , vol.211 , pp. 1-6
    • Lambert, S.1    Bennett, V.2
  • 45
    • 0027337107 scopus 로고
    • R-spectrin in discrete neuronal populations of the rat brain
    • R-spectrin in discrete neuronal populations of the rat brain. J. Neurosci. 13:3725-3735.
    • (1993) J. Neurosci. , vol.13 , pp. 3725-3735
    • Lambert, S.1    Bennett, V.2
  • 47
    • 10544223213 scopus 로고
    • Ankyrin clustering in the coordinate recruitment of ion channels and adhesion molecules during morphogenesis of the node of Ranvier
    • Lambert, S., J. Davis, P. Michaely, and V. Bennett. 1995. Ankyrin clustering in the coordinate recruitment of ion channels and adhesion molecules during morphogenesis of the node of Ranvier. Mol. Biol. Cell. 6:98a.
    • (1995) Mol. Biol. Cell. , vol.6
    • Lambert, S.1    Davis, J.2    Michaely, P.3    Bennett, V.4
  • 49
    • 0003147477 scopus 로고
    • Disorders of the red cell membrane
    • R.I. Handin, S.E. Lux, and T.P. Stossel, editors. J.B. Lippincott Co., Philadelphia
    • Lux, S.E., and J. Palek. 1995. Disorders of the red cell membrane. In Blood: Principles and Practice of Hematology. R.I. Handin, S.E. Lux, and T.P. Stossel, editors. J.B. Lippincott Co., Philadelphia. 1701-1808.
    • (1995) Blood: Principles and Practice of Hematology , pp. 1701-1808
    • Lux, S.E.1    Palek, J.2
  • 50
    • 0025117790 scopus 로고
    • Analysis of cDNA for human erythrocyte ankyrin indicates a repeated structure with homology to tissue-differentiation and cell-cycle control proteins
    • Lux, S.E., K.M. John, and V. Bennett. 1990. Analysis of cDNA for human erythrocyte ankyrin indicates a repeated structure with homology to tissue-differentiation and cell-cycle control proteins. Nature. 344:36-42.
    • (1990) Nature , vol.344 , pp. 36-42
    • Lux, S.E.1    John, K.M.2    Bennett, V.3
  • 51
    • 0028121111 scopus 로고
    • Expression and functional roles of neuronal cell adhesion molecules and extracellular matrix components during development and regeneration of peripheral nerves
    • Martini, R. 1994. Expression and functional roles of neuronal cell adhesion molecules and extracellular matrix components during development and regeneration of peripheral nerves. J. Neurocytol. 23:1-28.
    • (1994) J. Neurocytol. , vol.23 , pp. 1-28
    • Martini, R.1
  • 52
    • 0026529403 scopus 로고
    • Phosphorylation-dependent neurofilament epitopes are reduced as the node of Ranvier
    • Mata, M., N. Kupina, and D.J. Fink. 1992. Phosphorylation-dependent neurofilament epitopes are reduced as the node of Ranvier. J. Neurocytol. 21:199-210.
    • (1992) J. Neurocytol. , vol.21 , pp. 199-210
    • Mata, M.1    Kupina, N.2    Fink, D.J.3
  • 54
    • 0026607234 scopus 로고
    • ANK repeats: A ubiquitous motif involved in macromolecular recognition
    • Michaely, P., and V. Bennett. 1992. ANK repeats: a ubiquitous motif involved in macromolecular recognition. Trends Cell Biol. 2:127-129.
    • (1992) Trends Cell Biol. , vol.2 , pp. 127-129
    • Michaely, P.1    Bennett, V.2
  • 55
    • 0027374511 scopus 로고
    • The membrane-binding domain of ankyrin contains four independently-folded subdomains each comprised of six ankyrin repeats
    • Michaely, P., and V. Bennett. 1993. The membrane-binding domain of ankyrin contains four independently-folded subdomains each comprised of six ankyrin repeats. J. Biol. Chem. 268:22703-22709.
    • (1993) J. Biol. Chem. , vol.268 , pp. 22703-22709
    • Michaely, P.1    Bennett, V.2
  • 56
    • 0029150191 scopus 로고
    • The ANK repeats of erythrocyte ankyrin form two distinct but cooperative binding sites for the erythrocyte anion exchanger
    • Michaely, P., and V. Bennett. 1995a. The ANK repeats of erythrocyte ankyrin form two distinct but cooperative binding sites for the erythrocyte anion exchanger. J. Biol. Chem. 270:22050-22057.
    • (1995) J. Biol. Chem. , vol.270 , pp. 22050-22057
    • Michaely, P.1    Bennett, V.2
  • 58
    • 0027723273 scopus 로고
    • Induction of axonal growth by heterophilic interactions between the cell surface recognition proteins F11 and Nr-CAM/Bravo
    • Morales, G., M. Hubert, T. Brummendorf, U. Treubert, A. Tarnok, U. Schwarz, and F. Rathgen. 1993. Induction of axonal growth by heterophilic interactions between the cell surface recognition proteins F11 and Nr-CAM/Bravo. Neuron. 11:1113-1122.
    • (1993) Neuron , vol.11 , pp. 1113-1122
    • Morales, G.1    Hubert, M.2    Brummendorf, T.3    Treubert, U.4    Tarnok, A.5    Schwarz, U.6    Rathgen, F.7
  • 59
    • 0023262074 scopus 로고
    • +) ATPase and implications for the organization of membrane domains in polarized cells
    • +) ATPase and implications for the organization of membrane domains in polarized cells. Nature. 328:533-535.
    • (1987) Nature , vol.328 , pp. 533-535
    • Nelson, W.J.1    Veshnock, P.J.2
  • 61
    • 0025874185 scopus 로고
    • Isolation and characterization of cDNAs encoding human brain ankyrins reveal a family of alternatively-spliced genes
    • Otto, E., M. Kunimoto, T. McLaughlin, and V. Bennett. 1991. Isolation and characterization of cDNAs encoding human brain ankyrins reveal a family of alternatively-spliced genes. J. Cell Biol. 114:241-253.
    • (1991) J. Cell Biol. , vol.114 , pp. 241-253
    • Otto, E.1    Kunimoto, M.2    McLaughlin, T.3    Bennett, V.4
  • 63
    • 0029047129 scopus 로고
    • Ank3 (epithelial ankyrin), a widely distributed new member of the ankyrin gene family and the major ankyrin in kidney, is expressed in alternatively spliced forms, including forms that lack the repeat domain
    • Peters, L.L., K.M. John, P.M. Lu, E.M. Eicher, A. Higgins, M. Yialamas, L.C. Turtzo, A. Otsuka, and S.E. Lux. 1995. Ank3 (epithelial ankyrin), a widely distributed new member of the ankyrin gene family and the major ankyrin in kidney, is expressed in alternatively spliced forms, including forms that lack the repeat domain. J. Cell Biol. 130:313-321.
    • (1995) J. Cell Biol. , vol.130 , pp. 313-321
    • Peters, L.L.1    John, K.M.2    Lu, P.M.3    Eicher, E.M.4    Higgins, A.5    Yialamas, M.6    Turtzo, L.C.7    Otsuka, A.8    Lux, S.E.9
  • 64
    • 0002427587 scopus 로고
    • De quelque faits relatifs a l'histologie et a la physiologique des muscl stries
    • Ranvier, L. 1874. De quelque faits relatifs a l'histologie et a la physiologique des muscl stries. Arch. Physiol. Norm. Path. 2(Ser.1):5-15.
    • (1874) Arch. Physiol. Norm. Path. , vol.2 , Issue.SER.1 , pp. 5-15
    • Ranvier, L.1
  • 65
    • 0000143250 scopus 로고
    • Glycoproteins that regulate the growth and guidance of vertebrate axons: Domains and dynamics of the immunoglobulin/fibronectin type III subfamily
    • Rathjen, F.G., and T.M. Jessel. 1991. Glycoproteins that regulate the growth and guidance of vertebrate axons: domains and dynamics of the immunoglobulin/fibronectin type III subfamily. Semin. Neurosci. 3:297-307.
    • (1991) Semin. Neurosci. , vol.3 , pp. 297-307
    • Rathjen, F.G.1    Jessel, T.M.2
  • 66
    • 0013647625 scopus 로고
    • Preliminary observations on the ultrastructure of nodes of Ranvier
    • Robertson, J.D. 1959. Preliminary observations on the ultrastructure of nodes of Ranvier. Z. Zellforsch. Mikrosk. Anat. 50:553-560.
    • (1959) Z. Zellforsch. Mikrosk. Anat. , vol.50 , pp. 553-560
    • Robertson, J.D.1
  • 67
    • 0027511472 scopus 로고
    • Overt diabetic neuropathy: Repair of axo-glial dysjunction and axonal atrophy by aldose reductase inhibition and its correlation to improvement in nerve conduction velocity
    • Sima, A.A., A. Prasher, V. Nathaniel, M.R. Werb, and D.A. Greene. 1993. Overt diabetic neuropathy: repair of axo-glial dysjunction and axonal atrophy by aldose reductase inhibition and its correlation to improvement in nerve conduction velocity. Diabetic Med. 10:115-121.
    • (1993) Diabetic Med. , vol.10 , pp. 115-121
    • Sima, A.A.1    Prasher, A.2    Nathaniel, V.3    Werb, M.R.4    Greene, D.A.5
  • 68
    • 0027096397 scopus 로고
    • Regulation of axonal growth in the vertebrate nervous system by interactions between glycoproteins belonging to two subgroups of the immunoglobulin superfamily
    • Sonderegger, P., and F.G. Rathgen. 1992. Regulation of axonal growth in the vertebrate nervous system by interactions between glycoproteins belonging to two subgroups of the immunoglobulin superfamily. J. Cell Biol. 119:1387-1394.
    • (1992) J. Cell Biol. , vol.119 , pp. 1387-1394
    • Sonderegger, P.1    Rathgen, F.G.2
  • 69
    • 0023948543 scopus 로고
    • Ankyrin and spectrin associate with voltage-dependent sodium channels in brain
    • Srinivasan, Y., L. Elmer, J. Davis, V. Bennett, and K. Angelides. 1988. Ankyrin and spectrin associate with voltage-dependent sodium channels in brain. Nature. 333:177-180.
    • (1988) Nature , vol.333 , pp. 177-180
    • Srinivasan, Y.1    Elmer, L.2    Davis, J.3    Bennett, V.4    Angelides, K.5
  • 70
    • 0024521890 scopus 로고
    • Co-localization of the myelin-associated glycoprotein and the microfilament components, F-actin and spectrin, in Schwann cells of myelinated nerve fibers
    • Trapp, B.D., S.B. Andrews, A. Wong, M. O'Connell, and J.W. Griffin. 1989. Co-localization of the myelin-associated glycoprotein and the microfilament components, F-actin and spectrin, in Schwann cells of myelinated nerve fibers. J. Neurocytol. 18:47-60.
    • (1989) J. Neurocytol. , vol.18 , pp. 47-60
    • Trapp, B.D.1    Andrews, S.B.2    Wong, A.3    O'Connell, M.4    Griffin, J.W.5
  • 71
    • 0026582830 scopus 로고
    • Ultrastructural concomitants of anoxic injury and early post-anoxic recovery in rat optic nerve
    • Waxman, S.G., J.A. Black, P.K. Stys, and B.R. Ransom. 1992. Ultrastructural concomitants of anoxic injury and early post-anoxic recovery in rat optic nerve. Brain Res. 574:105-119.
    • (1992) Brain Res. , vol.574 , pp. 105-119
    • Waxman, S.G.1    Black, J.A.2    Stys, P.K.3    Ransom, B.R.4
  • 72
    • 0027398432 scopus 로고
    • Molecular dissection of the myelinated axon
    • Waxman, S.G., and J.M. Ritchie. 1993. Molecular dissection of the myelinated axon. Ann. Neurol. 33:121-136.
    • (1993) Ann. Neurol. , vol.33 , pp. 121-136
    • Waxman, S.G.1    Ritchie, J.M.2
  • 73
    • 0028029162 scopus 로고
    • Activation of the FGF receptor underlies neurite outgrowth stimulated by L1, N-CAM and N-cadherin
    • Williams, E.J., J. Furness, F.S. Walsh, and P. Doherty. 1994. Activation of the FGF receptor underlies neurite outgrowth stimulated by L1, N-CAM and N-cadherin. Neuron. 13:583-594.
    • (1994) Neuron , vol.13 , pp. 583-594
    • Williams, E.J.1    Furness, J.2    Walsh, F.S.3    Doherty, P.4
  • 74
    • 0026718372 scopus 로고
    • Structure of the axonal surface recognition molecule neurofascin and its relationship to a neural subgroup of the immunoglobulin superfamily
    • Volkmer, H., B. Hassel, J.M. Wolff, R. Frank, and F.G. Rathjen. 1992. Structure of the axonal surface recognition molecule neurofascin and its relationship to a neural subgroup of the immunoglobulin superfamily. J. Cell Biol. 118:149-161.
    • (1992) J. Cell Biol. , vol.118 , pp. 149-161
    • Volkmer, H.1    Hassel, B.2    Wolff, J.M.3    Frank, R.4    Rathjen, F.G.5
  • 75
    • 0029969728 scopus 로고    scopus 로고
    • G isoforms targeted to nodes of Ranvier
    • G isoforms targeted to nodes of Ranvier. J. Biol. Chem. 271:31391-31398.
    • (1996) J. Biol. Chem. , vol.271 , pp. 31391-31398
    • Zhang, X.1    Bennett, V.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.