메뉴 건너뛰기




Volumn 8, Issue 4, 1998, Pages 771-793

Mouse models of myelin diseases

Author keywords

[No Author keywords available]

Indexed keywords

ANIMAL MODEL; CONFERENCE PAPER; DEMYELINATING DISEASE; GENE MUTATION; GENETIC TRANSCRIPTION; MYELINATION; NEUROPATHOLOGY; NONHUMAN; OLIGODENDROGLIA; SCHWANN CELL;

EID: 0031659692     PISSN: 10156305     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1750-3639.1998.tb00200.x     Document Type: Conference Paper
Times cited : (47)

References (194)
  • 2
    • 0030994297 scopus 로고    scopus 로고
    • Heterozygous peripheral myelin protein 22-deficient mice are affected by a progressive demyelinating tomaculous neuropathy
    • Adlkofer K, Frei R, Neuberg DH, Zielasek J, Toyka KV, Suter U (1997) Heterozygous peripheral myelin protein 22-deficient mice are affected by a progressive demyelinating tomaculous neuropathy. J Neurosci 17:4662-4671
    • (1997) J Neurosci , vol.17 , pp. 4662-4671
    • Adlkofer, K.1    Frei, R.2    Neuberg, D.H.3    Zielasek, J.4    Toyka, K.V.5    Suter, U.6
  • 3
    • 0030883723 scopus 로고    scopus 로고
    • Analysis of compound heterozygous mice reveals that the Trembler mutation can behave as a gain-of-function allele
    • Adlkofer K, Naef R, Suter U (1997) Analysis of compound heterozygous mice reveals that the Trembler mutation can behave as a gain-of-function allele. J Neurosci Res 49:671-680
    • (1997) J Neurosci Res , vol.49 , pp. 671-680
    • Adlkofer, K.1    Naef, R.2    Suter, U.3
  • 4
    • 0030795612 scopus 로고    scopus 로고
    • The ErbB signaling network in embryogenesis and oncogenesis: Signal diversification through combinatorial ligand-receptor interactions
    • Alroy I, Yarden Y (1997) The ErbB signaling network in embryogenesis and oncogenesis: signal diversification through combinatorial ligand-receptor interactions. FEBS Lett 410:83-86
    • (1997) FEBS Lett , vol.410 , pp. 83-86
    • Alroy, I.1    Yarden, Y.2
  • 6
    • 0030979840 scopus 로고    scopus 로고
    • Structural abnormalities and deficient maintenance of peripheral nerve myetin in mice lacking the gap junction protein connexin 32
    • Anzini P, Neuberg DH, Schachner M, Nelles E, Willecke K, Zielasek J, Toyka KV, Suter U, Martini R (1997) Structural abnormalities and deficient maintenance of peripheral nerve myetin in mice lacking the gap junction protein connexin 32. J Neurosci 17:4545-4551
    • (1997) J Neurosci , vol.17 , pp. 4545-4551
    • Anzini, P.1    Neuberg, D.H.2    Schachner, M.3    Nelles, E.4    Willecke, K.5    Zielasek, J.6    Toyka, K.V.7    Suter, U.8    Martini, R.9
  • 8
    • 0030742643 scopus 로고    scopus 로고
    • Increased number of unmyelinated axons in optic nerves of adult mice deficient in the myelin-associated glycoprotein (MAG)
    • Bartsch S, Montag D, Schachner M, Bartsch U (1997) Increased number of unmyelinated axons in optic nerves of adult mice deficient in the myelin-associated glycoprotein (MAG) Brain Res 762:231-234
    • (1997) Brain Res , vol.762 , pp. 231-234
    • Bartsch, S.1    Montag, D.2    Schachner, M.3    Bartsch, U.4
  • 9
    • 0028941681 scopus 로고
    • Igf1 gene disruption results in reduced brain size, CNS hypomyelination, and ioss of hippocampal granule and striatal parvalbumin-containing neurons
    • Beck KD, Powell-Braxton L, Widmer HR, Valverde J, Hefti F (1995) Igf1 gene disruption results in reduced brain size, CNS hypomyelination, and ioss of hippocampal granule and striatal parvalbumin-containing neurons. Neuron 14:717-730
    • (1995) Neuron , vol.14 , pp. 717-730
    • Beck, K.D.1    Powell-Braxton, L.2    Widmer, H.R.3    Valverde, J.4    Hefti, F.5
  • 10
    • 0028566461 scopus 로고
    • X-linked adrenoleukodystrophy (ALD): A novel mutation of the ALD gene in 6 members of a family presenting with 5 different phenotypes
    • Berger J, Molzer B, Fae I, Bernheimer H (1994) X-linked adrenoleukodystrophy (ALD): a novel mutation of the ALD gene in 6 members of a family presenting with 5 different phenotypes. Biochem Biophys Res Commun 205:1638-1643
    • (1994) Biochem Biophys Res Commun , vol.205 , pp. 1638-1643
    • Berger, J.1    Molzer, B.2    Fae, I.3    Bernheimer, H.4
  • 13
    • 0027986675 scopus 로고
    • Disruption of the compacted myelin sheath of axons of the central nervous system in proteolipid protein-deficient mice
    • Boison D, Stoffel W (1994) Disruption of the compacted myelin sheath of axons of the central nervous system in proteolipid protein-deficient mice. Proc Natl Acad Sci (USA) 91: 11709-11713
    • (1994) Proc Natl Acad Sci (USA) , vol.91 , pp. 11709-11713
    • Boison, D.1    Stoffel, W.2
  • 14
    • 0029127508 scopus 로고
    • Adhesive properties of proteolipid protein are responsible for the compaction of CNS myelin sheaths
    • Boison D, Bussow H, D'Urso D, Muller HW, Stoffel W (1995) Adhesive properties of proteolipid protein are responsible for the compaction of CNS myelin sheaths. J Neurosci 5:5502-5513
    • (1995) J Neurosci , vol.5 , pp. 5502-5513
    • Boison, D.1    Bussow, H.2    D'Urso, D.3    Muller, H.W.4    Stoffel, W.5
  • 16
    • 0029851157 scopus 로고    scopus 로고
    • Functional breakdown of the lipid bilayer of the myelin membrane in central and peripheral nervous system by disrupted galactocerebroside synthesis
    • Bosio A, Binczek E, Stoffel W (1996) Functional breakdown of the lipid bilayer of the myelin membrane in central and peripheral nervous system by disrupted galactocerebroside synthesis. Proc Natl Acad Sci (USA) 93: 13280-13285
    • (1996) Proc Natl Acad Sci (USA) , vol.93 , pp. 13280-13285
    • Bosio, A.1    Binczek, E.2    Stoffel, W.3
  • 17
    • 0031982356 scopus 로고    scopus 로고
    • Galactosphingolipids and axono-glial interaction in myelin of the central nervous system
    • Bosio A, Bussow H, Adam J, Stoffel W (1998) Galactosphingolipids and axono-glial interaction in myelin of the central nervous system. Cell Tissue Res 292:199-210
    • (1998) Cell Tissue Res , vol.292 , pp. 199-210
    • Bosio, A.1    Bussow, H.2    Adam, J.3    Stoffel, W.4
  • 18
    • 0028018967 scopus 로고
    • Null mutations of connexin32 in patients with X-linked Charcot-Marie-Tooth disease
    • Bruzzone R, White TW, Scherer SS, Fischbeck KH, Paul DL (1994) Null mutations of connexin32 in patients with X-linked Charcot-Marie-Tooth disease. Neuron 13:1253-1260
    • (1994) Neuron , vol.13 , pp. 1253-1260
    • Bruzzone, R.1    White, T.W.2    Scherer, S.S.3    Fischbeck, K.H.4    Paul, D.L.5
  • 19
    • 0029923452 scopus 로고    scopus 로고
    • Three forms of RPTP-beta are differentially expressed during gliogenesis in the developing rat brain and during glial cell differentiation in culture
    • Canoll PD, Petanceska S, Schlessinger J, Musacchio JM (1996) Three forms of RPTP-beta are differentially expressed during gliogenesis in the developing rat brain and during glial cell differentiation in culture. J Neurosci Res 44:199-215
    • (1996) J Neurosci Res , vol.44 , pp. 199-215
    • Canoll, P.D.1    Petanceska, S.2    Schlessinger, J.3    Musacchio, J.M.4
  • 20
    • 0031022558 scopus 로고    scopus 로고
    • Absence of the myelin-associated glycoprotein (MAG) and the neural cell adhesion molecule (N-CAM) interferes with the maintenance, but not with the formation of peripheral myelin
    • Carenini S, Montag D, Cremer H, Schachner M, Martini R (1996) Absence of the myelin-associated glycoprotein (MAG) and the neural cell adhesion molecule (N-CAM) interferes with the maintenance, but not with the formation of peripheral myelin. Cell Tissue Res 287:3-9
    • (1996) Cell Tissue Res , vol.287 , pp. 3-9
    • Carenini, S.1    Montag, D.2    Cremer, H.3    Schachner, M.4    Martini, R.5
  • 22
    • 0030911331 scopus 로고    scopus 로고
    • Ligands for ErbB-family receptors encoded by a neuregulin-like gene
    • Chang H, Riese DJ 2nd, Gilbert W, Stern DF, McMahan UJ (1997) Ligands for ErbB-family receptors encoded by a neuregulin-like gene. Nature 387:509-512
    • (1997) Nature , vol.387 , pp. 509-512
    • Chang, H.1    Riese II, D.J.2    Gilbert, W.3    Stern, D.F.4    McMahan, U.J.5
  • 23
    • 0023675530 scopus 로고
    • A gene encoding a protein with zinc fingers is activated during GO/G1 in cultured cells
    • Chavrier P, Zerial M, Lemaire P, Almendral J, Bravo R, Charnay P (1988) A gene encoding a protein with zinc fingers is activated during GO/G1 in cultured cells. EMBO J 7:29-35
    • (1988) EMBO J , vol.7 , pp. 29-35
    • Chavrier, P.1    Zerial, M.2    Lemaire, P.3    Almendral, J.4    Bravo, R.5    Charnay, P.6
  • 24
    • 0031127216 scopus 로고    scopus 로고
    • cDNA cloning, genomic structure, and chromosome mapping of the human epithelial membrane protein CL-20 gene (EMP1), a member of the PMP22 family
    • Chen Y, Medvedev A, Ruzanov P, Marvin KW, Jetten AM (1997) cDNA cloning, genomic structure, and chromosome mapping of the human epithelial membrane protein CL-20 gene (EMP1), a member of the PMP22 family. Genomics 41:40-48
    • (1997) Genomics , vol.41 , pp. 40-48
    • Chen, Y.1    Medvedev, A.2    Ruzanov, P.3    Marvin, K.W.4    Jetten, A.M.5
  • 25
    • 0030602822 scopus 로고    scopus 로고
    • Myelination in the absence of galactocerebroside and sulfatide: Normal structure with abnormal function and regional instability
    • Coetzee T, Fujita N, Dupree J, Shi R, Blight A, Suzuki K, Suzuki K, Popko B (1996) Myelination in the absence of galactocerebroside and sulfatide: normal structure with abnormal function and regional instability Cell 86, 209-219
    • (1996) Cell , vol.86 , pp. 209-219
    • Coetzee, T.1    Fujita, N.2    Dupree, J.3    Shi, R.4    Blight, A.5    Suzuki, K.6    Suzuki, K.7    Popko, B.8
  • 26
    • 0032032415 scopus 로고    scopus 로고
    • New perspectives on the function of myelin galactolipids
    • Coetzee T, Suzuki K, Popko B (1998) New perspectives on the function of myelin galactolipids. Trends Neurosci 21:126-130
    • (1998) Trends Neurosci , vol.21 , pp. 126-130
    • Coetzee, T.1    Suzuki, K.2    Popko, B.3
  • 27
    • 0031195978 scopus 로고    scopus 로고
    • Signals that initiate myelination in the developing mammalian nervous system
    • Colello RJ, Pott U (1997) Signals that initiate myelination in the developing mammalian nervous system. Mol Neurobiol 15:83-100
    • (1997) Mol Neurobiol , vol.15 , pp. 83-100
    • Colello, R.J.1    Pott, U.2
  • 28
    • 0023493525 scopus 로고
    • An interstitial duplication of the X chromosome in a male allows physical fine mapping of probes from the Xq13-q22 region
    • Cremers FP, Pfeiffer RA, van de Pol TJ, Hofker MH, Kruse TA, Wieringa B, Ropers HH (1987) An interstitial duplication of the X chromosome in a male allows physical fine mapping of probes from the Xq13-q22 region. Hum Genet 77:23-27
    • (1987) Hum Genet , vol.77 , pp. 23-27
    • Cremers, F.P.1    Pfeiffer, R.A.2    Van de Pol, T.J.3    Hofker, M.H.4    Kruse, T.A.5    Wieringa, B.6    Ropers, H.H.7
  • 29
    • 0025253083 scopus 로고
    • Protein zero of peripheral nerve myelin: Biosynthesis, membrane insertion, and evidence for homotypic interaction
    • D'Urso D, Brophy PJ, Staugaitis SM, Gillespie CS, Frey AB, Stempak JG, Colman DR (1990) Protein zero of peripheral nerve myelin: biosynthesis, membrane insertion, and evidence for homotypic interaction. Neuron 4:449-460
    • (1990) Neuron , vol.4 , pp. 449-460
    • D'Urso, D.1    Brophy, P.J.2    Staugaitis, S.M.3    Gillespie, C.S.4    Frey, A.B.5    Stempak, J.G.6    Colman, D.R.7
  • 30
    • 1842333920 scopus 로고    scopus 로고
    • Ins and outs of peripheral myelin protein-22: Mapping transmembrane topology and intracellular sorting
    • D'Urso D, Müller HW (1997) Ins and outs of peripheral myelin protein-22: mapping transmembrane topology and intracellular sorting. J Neurosci Res 49:551-562
    • (1997) J Neurosci Res , vol.49 , pp. 551-562
    • D'Urso, D.1    Müller, H.W.2
  • 31
    • 0030887142 scopus 로고    scopus 로고
    • Studies on the effects of altered PMP22 expression during myelination in vitro
    • D'Urso D, Schmalenbach C, Zoidl G, Pnor R, Muller HW (1997) Studies on the effects of altered PMP22 expression during myelination in vitro. J Neurosci Res 48:31-42
    • (1997) J Neurosci Res , vol.48 , pp. 31-42
    • D'Urso, D.1    Schmalenbach, C.2    Zoidl, G.3    Pnor, R.4    Muller, H.W.5
  • 32
    • 0031972929 scopus 로고    scopus 로고
    • Overloaded endoplasmic reticulumGolgi compartments, a possible pathomechanism of peripheral neuropathies caused by mutations of the peripheral myelin protein PMP22
    • D'Urso D, Prior R, Greiner-Petter R, Gabreels-Festen AA, Muller HW (1998) Overloaded endoplasmic reticulumGolgi compartments, a possible pathomechanism of peripheral neuropathies caused by mutations of the peripheral myelin protein PMP22. J Neurosci 18:731-740
    • (1998) J Neurosci , vol.18 , pp. 731-740
    • D'Urso, D.1    Prior, R.2    Greiner-Petter, R.3    Gabreels-Festen, A.A.4    Muller, H.W.5
  • 33
    • 0023334485 scopus 로고
    • Lonophoric properties of the proteolipid apoprotein from bovine brain myelin
    • de Cozar M, Lucas M, Monreal J (1987) lonophoric properties of the proteolipid apoprotein from bovine brain myelin. Biochem Int 14:833-841
    • (1987) Biochem Int , vol.14 , pp. 833-841
    • De Cozar, M.1    Lucas, M.2    Monreal, J.3
  • 34
    • 0025073861 scopus 로고
    • Calcium movements mediated by proteolipid protein and nucleotides in liposomes prepared with the endogenous lipids from brain white matter
    • Diaz RS, Monreal J, Lucas M (1990) Calcium movements mediated by proteolipid protein and nucleotides in liposomes prepared with the endogenous lipids from brain white matter. J Neurochem 55:1304-1309
    • (1990) J Neurochem , vol.55 , pp. 1304-1309
    • Diaz, R.S.1    Monreal, J.2    Lucas, M.3
  • 35
    • 0028244197 scopus 로고
    • The cytoplasmic domain of myelin glycoprotein PO interacts with negatively charged phospholipid bilayers
    • Ding Y, Brunden KR (1994) The cytoplasmic domain of myelin glycoprotein PO interacts with negatively charged phospholipid bilayers. J Biol Chem 269:10764-10770
    • (1994) J Biol Chem , vol.269 , pp. 10764-10770
    • Ding, Y.1    Brunden, K.R.2
  • 36
    • 0027679338 scopus 로고
    • Glial-neuron interactions and the regulation of myelin formation
    • Doyle JP, Colman DR (1993) Glial-neuron interactions and the regulation of myelin formation. Curr Opin Cell Biol 5:779-785
    • (1993) Curr Opin Cell Biol , vol.5 , pp. 779-785
    • Doyle, J.P.1    Colman, D.R.2
  • 37
    • 0023404814 scopus 로고
    • Abnormal compact myelin in the myelin-deficient rat absence of proteolipid protein correlates with a defect in the intraperiod line
    • Duncan ID, Hammang JP, Trapp BD (1987) Abnormal compact myelin in the myelin-deficient rat absence of proteolipid protein correlates with a defect in the intraperiod line. Proc Natl Acad Sci U S A 84:6287-6291
    • (1987) Proc Natl Acad Sci U S A , vol.84 , pp. 6287-6291
    • Duncan, I.D.1    Hammang, J.P.2    Trapp, B.D.3
  • 38
    • 0024585529 scopus 로고
    • Myelination in the jimpy mouse in the absence of proteclipid protein
    • Duncan ID, Hammang JP, Goda S, Quarles RH (1989) Myelination in the jimpy mouse in the absence of proteclipid protein. Glia 2:148-154
    • (1989) Glia , vol.2 , pp. 148-154
    • Duncan, I.D.1    Hammang, J.P.2    Goda, S.3    Quarles, R.H.4
  • 39
    • 0032031635 scopus 로고    scopus 로고
    • Myelin galactolipids are essential for proper node of Ranvier formation in the CNS
    • Dupree JL, Coetzee T, Blight A, Suzuki K, Popko B (1998) Myelin galactolipids are essential for proper node of Ranvier formation in the CNS. J Neurosci 18: 1642-1649
    • (1998) J Neurosci , vol.18 , pp. 1642-1649
    • Dupree, J.L.1    Coetzee, T.2    Blight, A.3    Suzuki, K.4    Popko, B.5
  • 41
    • 0031453392 scopus 로고    scopus 로고
    • The axonal membrane protein Caspr, a homologue of neurexin IV, is a component of the septate-like paranodal junctions that assemble during myelination
    • Einheber S, Zanazzi G, Ching W. Scherer S, Milner TA, Peles E, Salzer JL (1997) The axonal membrane protein Caspr, a homologue of neurexin IV, is a component of the septate-like paranodal junctions that assemble during myelination. J Cell Biol 139:1495-1506
    • (1997) J Cell Biol , vol.139 , pp. 1495-1506
    • Einheber, S.1    Zanazzi, G.2    Ching, W.3    Scherer, S.4    Milner, T.A.5    Peles, E.6    Salzer, J.L.7
  • 42
    • 0028240173 scopus 로고
    • Proteolipid protein gene dosage effect in Pelizaeus-Merzbacher disease
    • Ellis D, Malcolm S (1994) Proteolipid protein gene dosage effect in Pelizaeus-Merzbacher disease . Nature Genet 6:333-334
    • (1994) Nature Genet , vol.6 , pp. 333-334
    • Ellis, D.1    Malcolm, S.2
  • 43
    • 0029159803 scopus 로고
    • Apoptotic phenotype induced by overexpression of wild-type gas3/PMP22: Its relation to the demyelinating peripheral neuropathy CMT1A
    • Fabbretti E, Edomi P, Brancolini C, Schneider C (1995) Apoptotic phenotype induced by overexpression of wild-type gas3/PMP22: its relation to the demyelinating peripheral neuropathy CMT1A. Genes Dev 9:1846-1856
    • (1995) Genes Dev , vol.9 , pp. 1846-1856
    • Fabbretti, E.1    Edomi, P.2    Brancolini, C.3    Schneider, C.4
  • 45
    • 0027261181 scopus 로고
    • Homophilic adhesion of the myelin PO protein requires glycosylation of both molecules in the homophilic pair
    • Filbin MT, Tennekoon GI (1993) Homophilic adhesion of the myelin PO protein requires glycosylation of both molecules in the homophilic pair. J Cell Biol 122:451-459
    • (1993) J Cell Biol , vol.122 , pp. 451-459
    • Filbin, M.T.1    Tennekoon, G.I.2
  • 48
    • 0031890416 scopus 로고    scopus 로고
    • Mouse strain backgrounds' more than black and white
    • Frankel WN (1998) Mouse strain backgrounds' more than black and white. Neuron 20:183
    • (1998) Neuron , vol.20 , pp. 183
    • Frankel, W.N.1
  • 49
    • 0028923245 scopus 로고
    • Crucial role for the myelin-associated glycoprotein in the maintenance of axon-myelin integrity
    • Fruttiger M, Montag D, Schachner M, Martini R (1995) Crucial role for the myelin-associated glycoprotein in the maintenance of axon-myelin integrity. Eur J Neurosci 7:511-515
    • (1995) Eur J Neurosci , vol.7 , pp. 511-515
    • Fruttiger, M.1    Montag, D.2    Schachner, M.3    Martini, R.4
  • 50
    • 0031471867 scopus 로고    scopus 로고
    • Gene dosage effects in hereditary peripheral neuropathy. Expression of peripheral myelin protein 22 inCharcot-Marie-Tooth disease type 1A and hereditaryneuropathy with liability to pressure palsies nerve biopsies
    • Gabriel JM, Erne B, Pareyson D, Sghirlanzoni A, Taroni F, Steck AJ (1997) Gene dosage effects in hereditary peripheral neuropathy. Expression of peripheral myelin protein 22 inCharcot-Marie-Tooth disease type 1A and hereditaryneuropathy with liability to pressure palsies nerve biopsies. Neurology 49:1635-1640
    • (1997) Neurology , vol.49 , pp. 1635-1640
    • Gabriel, J.M.1    Erne, B.2    Pareyson, D.3    Sghirlanzoni, A.4    Taroni, F.5    Steck, A.J.6
  • 52
    • 0029398501 scopus 로고
    • Clinical variability in two pairs of identical twins with the Charcot-Marie-Tooth disease type 1A duplication
    • Garcia CA, Malamut RE, England JD, Parry GS, Liu P, Lupski JR (1995) Clinical variability in two pairs of identical twins with the Charcot-Marie-Tooth disease type 1A duplication. Neurology 45:2090-2093
    • (1995) Neurology , vol.45 , pp. 2090-2093
    • Garcia, C.A.1    Malamut, R.E.2    England, J.D.3    Parry, G.S.4    Liu, P.5    Lupski, J.R.6
  • 53
    • 0031045328 scopus 로고    scopus 로고
    • Neuregulins and neuregulin receptors in neural development
    • Gassmann M, Lemke G (1997) Neuregulins and neuregulin receptors in neural development. Curr Opin Neurobiol 7:87-92
    • (1997) Curr Opin Neurobiol , vol.7 , pp. 87-92
    • Gassmann, M.1    Lemke, G.2
  • 55
    • 0025176499 scopus 로고
    • Conservative amino acid substitution in the myelin proteolipid protein of jimpymsd mice
    • Gencic S, Hudson LD (1990) Conservative amino acid substitution in the myelin proteolipid protein of jimpymsd mice. J Neurosci 10:117-124
    • (1990) J Neurosci , vol.10 , pp. 117-124
    • Gencic, S.1    Hudson, L.D.2
  • 56
    • 0026615047 scopus 로고
    • Disruption of the PO gene in mice leads to abnormal expression of recognition molecules, and degeneration of myelin and axons
    • Giese KP, Martini R, Lemke G, Soriano P, Schachner M (1992) Disruption of the PO gene in mice leads to abnormal expression of recognition molecules, and degeneration of myelin and axons. Cell 71:565-576
    • (1992) Cell , vol.71 , pp. 565-576
    • Giese, K.P.1    Martini, R.2    Lemke, G.3    Soriano, P.4    Schachner, M.5
  • 57
    • 0028226949 scopus 로고
    • Many naturally occurring mutations of myelin proteolipid protein impair its intracellular transport
    • Gow A, Friedrich VL, Lazzarini RA (1994) Many naturally occurring mutations of myelin proteolipid protein impair its intracellular transport. J Neurosci Res 37:574-583
    • (1994) J Neurosci Res , vol.37 , pp. 574-583
    • Gow, A.1    Friedrich, V.L.2    Lazzarini, R.A.3
  • 58
    • 0031025729 scopus 로고    scopus 로고
    • Conservation of topology, but not conformation, of the proteolipid proteins of the myelin sheath
    • Gow A, Gragerov A, Gard A, Colman DR, Lazzarini RA (1997) Conservation of topology, but not conformation, of the proteolipid proteins of the myelin sheath. J Neurosci 17:181-189
    • (1997) J Neurosci , vol.17 , pp. 181-189
    • Gow, A.1    Gragerov, A.2    Gard, A.3    Colman, D.R.4    Lazzarini, R.A.5
  • 59
    • 0030036917 scopus 로고    scopus 로고
    • A cellular mechanism governing the severity of Pelizaeus-Merzbacher disease
    • Gow A, Lazzarini RA (1996) A cellular mechanism governing the severity of Pelizaeus-Merzbacher disease. Nat Genet 13:422-428
    • (1996) Nat Genet , vol.13 , pp. 422-428
    • Gow, A.1    Lazzarini, R.A.2
  • 60
    • 0032559544 scopus 로고    scopus 로고
    • Disrupted proteolipid protein trafficking results in oligodendrocyte apoptosis in an animal model of Pelizaeus-Merzbacher disease
    • Gow A, Southwood CM, Lazzarini RA (1998) Disrupted proteolipid protein trafficking results in oligodendrocyte apoptosis in an animal model of Pelizaeus-Merzbacher disease. J Cell Biol 140:925-934
    • (1998) J Cell Biol , vol.140 , pp. 925-934
    • Gow, A.1    Southwood, C.M.2    Lazzarini, R.A.3
  • 61
    • 0030174240 scopus 로고    scopus 로고
    • Overexpression of 2′,3′-cyclic nucleotide 3′-phosphodiesterasein transgenic mice alters oligodendrocyte development and produces aberrant myelination
    • Gravel M, Peterson J, Yong VW, Kottis V, Trapp B, Braun PE (1996) Overexpression of 2′,3′-cyclic nucleotide 3′-phosphodiesterasein transgenic mice alters oligodendrocyte development and produces aberrant myelination. Mol Cell Neurosci 7:453-466
    • (1996) Mol Cell Neurosci , vol.7 , pp. 453-466
    • Gravel, M.1    Peterson, J.2    Yong, V.W.3    Kottis, V.4    Trapp, B.5    Braun, P.E.6
  • 62
  • 64
    • 0030250873 scopus 로고    scopus 로고
    • Onion bulb cells in mice deficient for myelin genes share molecular properties with immature, differentiated nonmyelinating, and denervated Schwann cells
    • Guenard V, Montag D, Schachner M, Martini R (1996) Onion bulb cells in mice deficient for myelin genes share molecular properties with immature, differentiated nonmyelinating, and denervated Schwann cells. Glia 18:27-38
    • (1996) Glia , vol.18 , pp. 27-38
    • Guenard, V.1    Montag, D.2    Schachner, M.3    Martini, R.4
  • 66
    • 0030791148 scopus 로고    scopus 로고
    • FGF plays a subtle role in oligodendrocyte maintenance in vivo
    • Harari D, Finkelstein D, Bernard O (1997) FGF plays a subtle role in oligodendrocyte maintenance in vivo. J Neurosci Res 49:404-415
    • (1997) J Neurosci Res , vol.49 , pp. 404-415
    • Harari, D.1    Finkelstein, D.2    Bernard, O.3
  • 67
    • 0023794823 scopus 로고
    • Long lives for homozygous trembler mutant mice despite virtual absence of peripheral nerve myelin
    • Henry EW, Sidman RL (1988) Long lives for homozygous trembler mutant mice despite virtual absence of peripheral nerve myelin. Science 241 344-346
    • (1988) Science , vol.241 , pp. 344-346
    • Henry, E.W.1    Sidman, R.L.2
  • 68
    • 0029980997 scopus 로고    scopus 로고
    • The proteolipid protein gene: Double, double. . . . and trouble
    • Hodes ME, Dlouhy SR (1996) The proteolipid protein gene: double, double. . . . and trouble. Am J Hum Genet 59: 12-15
    • (1996) Am J Hum Genet , vol.59 , pp. 12-15
    • Hodes, M.E.1    Dlouhy, S.R.2
  • 70
    • 0030273263 scopus 로고    scopus 로고
    • The L1 family of neural cell adhesion molecules: Old proteins performing new tricks
    • Hortsch M (1996) The L1 family of neural cell adhesion molecules: old proteins performing new tricks. Neuron 17:587-593
    • (1996) Neuron , vol.17 , pp. 587-593
    • Hortsch, M.1
  • 76
    • 0028893387 scopus 로고
    • Over-expression of the DM-20 myelin proteolipid causes central nervous system demyelination in transgenic mice
    • Johnson RS, Roder JC, Riordan JR (1995) Over-expression of the DM-20 myelin proteolipid causes central nervous system demyelination in transgenic mice. J Neurochem 64:967-976
    • (1995) J Neurochem , vol.64 , pp. 967-976
    • Johnson, R.S.1    Roder, J.C.2    Riordan, J.R.3
  • 77
    • 3042909761 scopus 로고
    • Dominant-negative action of mutations in the PLP/DM-20 gene and direct interaction of PLP polypeptides in vivo
    • Jung M, Schneider A, Nave KA (1995) Dominant-negative action of mutations in the PLP/DM-20 gene and direct interaction of PLP polypeptides in vivo. J Neurochem 64:S101.
    • (1995) J Neurochem , vol.64
    • Jung, M.1    Schneider, A.2    Nave, K.A.3
  • 78
    • 0029845073 scopus 로고    scopus 로고
    • Monoclonal antibody O10 defines a conformationally sensitive cell- Surface epitope of proteolipid protein (PLP)' evidence that PLP misfolding underlies dysmyelination in mutant mice
    • Jung M, Sommer I, Schachner M, Nave KA (1996) Monoclonal antibody O10 defines a conformationally sensitive cell- surface epitope of proteolipid protein (PLP)' evidence that PLP misfolding underlies dysmyelination in mutant mice J Neurosci 16:7920-7929
    • (1996) J Neurosci , vol.16 , pp. 7920-7929
    • Jung, M.1    Sommer, I.2    Schachner, M.3    Nave, K.A.4
  • 79
    • 0031053137 scopus 로고    scopus 로고
    • The cell adhesion molecule L1: Species- And cell-type-dependent multiple binding mechanisms
    • Kadmon G, Altevogt P (1997) The cell adhesion molecule L1: species- and cell-type-dependent multiple binding mechanisms. Differentiation 61:143-150
    • (1997) Differentiation , vol.61 , pp. 143-150
    • Kadmon, G.1    Altevogt, P.2
  • 81
    • 0028131358 scopus 로고
    • Elevated expression of messenger RNA for peripheral myelin protein 22 in biopsied peripheral nerves of patients with Charcot-Marie-Tooth disease type 1A
    • Kamholz J, Shy M, Scherer S (1994) Elevated expression of messenger RNA for peripheral myelin protein 22 in biopsied peripheral nerves of patients with Charcot-Marie-Tooth disease type 1A. Ann Neurol 36:451-452
    • (1994) Ann Neurol , vol.36 , pp. 451-452
    • Kamholz, J.1    Shy, M.2    Scherer, S.3
  • 83
    • 0029142724 scopus 로고
    • Pax3: A paired domain gene as a regulator in PNS myelination
    • Kioussi C, Gross MK, Gruss P (1995) Pax3: a paired domain gene as a regulator in PNS myelination. Neuron 15:553-562
    • (1995) Neuron , vol.15 , pp. 553-562
    • Kioussi, C.1    Gross, M.K.2    Gruss, P.3
  • 84
    • 0018835608 scopus 로고
    • Compact myelin exists in the absence of basic protein in the shiverer mutant mouse
    • Kirschner DA, Ganser, AL (1980) Compact myelin exists in the absence of basic protein in the shiverer mutant mouse. Nature 283:207-210
    • (1980) Nature , vol.283 , pp. 207-210
    • Kirschner, D.A.1    Ganser, A.L.2
  • 85
    • 0027424792 scopus 로고
    • A proteolipid protein gene family: Expression in sharks and rays and possible evolution from an ancestral gene encoding a pore-forming polypeptide
    • Kitagawa K, Sinoway MP, Yang C, Gould RM, Colman DR (1993) A proteolipid protein gene family: expression in sharks and rays and possible evolution from an ancestral gene encoding a pore-forming polypeptide. Neuron 11:433-448
    • (1993) Neuron , vol.11 , pp. 433-448
    • Kitagawa, K.1    Sinoway, M.P.2    Yang, C.3    Gould, R.M.4    Colman, D.R.5
  • 87
    • 0028236505 scopus 로고
    • The rumpshaker mutation in spastic paraplegia
    • Kobayashi H, Hoffman EP, Marks HG (1994) The rumpshaker mutation in spastic paraplegia. Nat Genet 7:351-352
    • (1994) Nat Genet , vol.7 , pp. 351-352
    • Kobayashi, H.1    Hoffman, E.P.2    Marks, H.G.3
  • 88
    • 0031587790 scopus 로고    scopus 로고
    • Adrenoleukodystrophy protein-deficient mice represent abnormality of very long chain fatty acid metabolism
    • Kobayashi T, Shinnoh N, Kondo A, Yamada T (1997) Adrenoleukodystrophy protein-deficient mice represent abnormality of very long chain fatty acid metabolism. Biochem Biophys Res Commun 232:631-636
    • (1997) Biochem Biophys Res Commun , vol.232 , pp. 631-636
    • Kobayashi, T.1    Shinnoh, N.2    Kondo, A.3    Yamada, T.4
  • 89
    • 0031104743 scopus 로고    scopus 로고
    • Expression of the immunoglobulin superfamily cell adhesion molecule F3 by oligodendrocyte-lineage cells
    • Koch T, Brugger T, Bach A, Gennarini G, Trotter J (1997) Expression of the immunoglobulin superfamily cell adhesion molecule F3 by oligodendrocyte-lineage cells. Glia 19: 199-212
    • (1997) Glia , vol.19 , pp. 199-212
    • Koch, T.1    Brugger, T.2    Bach, A.3    Gennarini, G.4    Trotter, J.5
  • 91
    • 0030742989 scopus 로고    scopus 로고
    • Variability of endocrinological dysfunction in 55 patients with X-linked adrenoleucodystrophy: Clinical, laboratory and genetic findings
    • Korenke GC, Roth C, Krasemann E, Hufner M, Hunneman DH, Hanefeld F (1997) Variability of endocrinological dysfunction in 55 patients with X-linked adrenoleucodystrophy: clinical, laboratory and genetic findings. Eur J Endocrinol 137:40-47
    • (1997) Eur J Endocrinol , vol.137 , pp. 40-47
    • Korenke, G.C.1    Roth, C.2    Krasemann, E.3    Hufner, M.4    Hunneman, D.H.5    Hanefeld, F.6
  • 93
    • 0031081587 scopus 로고    scopus 로고
    • Dying-back oligodendrogliopathy: A late sequel of myelin-associated glycoprotein deficiency
    • Lassmann H, Bartsch U, Montag D, Schachner M (1997) Dying-back oligodendrogliopathy: a late sequel of myelin-associated glycoprotein deficiency. Glia 19:104-110
    • (1997) Glia , vol.19 , pp. 104-110
    • Lassmann, H.1    Bartsch, U.2    Montag, D.3    Schachner, M.4
  • 94
    • 0000029565 scopus 로고
    • Proteins of myelin
    • (Ed. Morrell P) Plenum Press, New York
    • Lees MB, Brostoff SW (1984) Proteins of myelin. In: Myelin (Ed. Morrell P) 197-224, Plenum Press, New York
    • (1984) Myelin , pp. 197-224
    • Lees, M.B.1    Brostoff, S.W.2
  • 95
    • 0021849731 scopus 로고
    • Isolation and sequence of a cDNA encoding the major structural protein of peripheral myelin
    • Lemke G, Axel R (1985) isolation and sequence of a cDNA encoding the major structural protein of peripheral myelin. Cell 40:501-508
    • (1985) Cell , vol.40 , pp. 501-508
    • Lemke, G.1    Axel, R.2
  • 96
    • 0032518366 scopus 로고    scopus 로고
    • Myelin associated glycoprotein modulates glia-axon contact in vivo
    • Li C, Trapp B, Ludwin S, Peterson A, Roder J (1998) Myelin associated glycoprotein modulates glia-axon contact in vivo. J Neurosci Res 51:210-217
    • (1998) J Neurosci Res , vol.51 , pp. 210-217
    • Li, C.1    Trapp, B.2    Ludwin, S.3    Peterson, A.4    Roder, J.5
  • 98
    • 0032519751 scopus 로고    scopus 로고
    • Apoptotic glial cell death and kinetics in the spinal cord of the myelin-deficient rat
    • Lipsitz D, Goetz BD, Duncan ID (1998) Apoptotic glial cell death and kinetics in the spinal cord of the myelin-deficient rat. J Neurosci Res 51:497-507
    • (1998) J Neurosci Res , vol.51 , pp. 497-507
    • Lipsitz, D.1    Goetz, B.D.2    Duncan, I.D.3
  • 100
    • 0030034602 scopus 로고    scopus 로고
    • A close relative of the adrenoleukodystrophy (ALD) gene codes for a peroxisomal protein with a specific expression pattern
    • Lombard-Platet G, Savary S, Sarde CO, Mandel JL, Chimini G (1996) A close relative of the adrenoleukodystrophy (ALD) gene codes for a peroxisomal protein with a specific expression pattern. Proc Natl Acad Sci U S A 93:1 265-1269
    • (1996) Proc Natl Acad Sci U S A , vol.93 , pp. 1265-1269
    • Lombard-Platet, G.1    Savary, S.2    Sarde, C.O.3    Mandel, J.L.4    Chimini, G.5
  • 102
    • 0031892597 scopus 로고    scopus 로고
    • Charcot-Marie-Tooth disease: Lessons in genetic mechanisms
    • Lupski JR (1998) Charcot-Marie-Tooth disease: lessons in genetic mechanisms. Mol Med 4: 3-11.
    • (1998) Mol Med , vol.4 , pp. 3-11
    • Lupski, J.R.1
  • 104
    • 0022976359 scopus 로고
    • Immunoelectron microscopic localization of neural cell adhesion molecules (L1, N-CAM, and MAG) and their shared carbohydrate epitope and myelin basic protein in developing sciatic nerve
    • Martini R, Schachner M (1986) Immunoelectron microscopic localization of neural cell adhesion molecules (L1, N-CAM, and MAG) and their shared carbohydrate epitope and myelin basic protein in developing sciatic nerve. J Cell Biol 103:2439-2448
    • (1986) J Cell Biol , vol.103 , pp. 2439-2448
    • Martini, R.1    Schachner, M.2
  • 105
    • 0029065654 scopus 로고
    • Mice doubly deficient in the genes for P0 and myelin basic protein show that both proteins contribute to the formation of the major dense line in peripheral nerve myelin
    • Martini R, Mohajen MH, Kasper S, Giese KP, Schachner M (1995a) Mice doubly deficient in the genes for P0 and myelin basic protein show that both proteins contribute to the formation of the major dense line in peripheral nerve myelin. J Neurosci 15:4488-4495
    • (1995) J Neurosci , vol.15 , pp. 4488-4495
    • Martini, R.1    Mohajen, M.H.2    Kasper, S.3    Giese, K.P.4    Schachner, M.5
  • 106
    • 0028824925 scopus 로고
    • Protein zero (P0)-deficient mice show myelin degeneration in peripheral nerves characteristic of inherited human neuropathies
    • Martini R, Zielasek J, Toyka KV, Giese KP, Schachner M (1995b) Protein zero (P0)-deficient mice show myelin degeneration in peripheral nerves characteristic of inherited human neuropathies Nature Genet 11:281-286
    • (1995) Nature Genet , vol.11 , pp. 281-286
    • Martini, R.1    Zielasek, J.2    Toyka, K.V.3    Giese, K.P.4    Schachner, M.5
  • 107
    • 0031128105 scopus 로고    scopus 로고
    • Molecular bases of myelin formation as revealed by investigations on mice deficient in glial cell surface molecules
    • Martini R, Schachner M (1997) Molecular bases of myelin formation as revealed by investigations on mice deficient in glial cell surface molecules. Glia 19:298-310
    • (1997) Glia , vol.19 , pp. 298-310
    • Martini, R.1    Schachner, M.2
  • 109
    • 0028827104 scopus 로고
    • Multiple essential functions of neuregulin in development
    • Meyer D, Birchmeier C (1995) Multiple essential functions of neuregulin in development. Nature 378:386-390
    • (1995) Nature , vol.378 , pp. 386-390
    • Meyer, D.1    Birchmeier, C.2
  • 111
    • 0022133330 scopus 로고
    • Nucleotide sequences of two mRNAs for rat brain myelin proteolipid protein
    • Milner RJ, Lai C, Nave KA, Lenoir D, Ogata J, Sutcliffe JG (1985) Nucleotide sequences of two mRNAs for rat brain myelin proteolipid protein. Cell 42:931-939
    • (1985) Cell , vol.42 , pp. 931-939
    • Milner, R.J.1    Lai, C.2    Nave, K.A.3    Lenoir, D.4    Ogata, J.5    Sutcliffe, J.G.6
  • 112
    • 1842356008 scopus 로고
    • Recombination within the myelin basic protein gene created the dysmyelinating shiverer mouse mutation
    • Molineaux SM, Engh H, de Ferra F, Hudson L, Lazzarini RA (1986) Recombination within the myelin basic protein gene created the dysmyelinating shiverer mouse mutation. Proc Natl Acad Sci U S A 83:7542-7546
    • (1986) Proc Natl Acad Sci U S A , vol.83 , pp. 7542-7546
    • Molineaux, S.M.1    Engh, H.2    De Ferra, F.3    Hudson, L.4    Lazzarini, R.A.5
  • 114
    • 0025149738 scopus 로고
    • Expression and activity of the POU transcription factor SCIP
    • Monuki ES, Kuhn R, Weinmaster G, Trapp BD, Lemke G (1990) Expression and activity of the POU transcription factor SCIP. Science 249:1300-1303
    • (1990) Science , vol.249 , pp. 1300-1303
    • Monuki, E.S.1    Kuhn, R.2    Weinmaster, G.3    Trapp, B.D.4    Lemke, G.5
  • 115
    • 0029088558 scopus 로고
    • Adrenoleukodystrophy: Molecular genetics, pathology, and Lorenzo's oil
    • Moser HW, Powers JM, Smith KD (1995) Adrenoleukodystrophy: molecular genetics, pathology, and Lorenzo's oil. Brain Pathol 5:259-266
    • (1995) Brain Pathol , vol.5 , pp. 259-266
    • Moser, H.W.1    Powers, J.M.2    Smith, K.D.3
  • 118
    • 0028017717 scopus 로고
    • A combination of PLP and DM20 transgenes promotes partial myelination in the jimpy mouse
    • Nadon NL, Arnheiter H, Hudson LD (1994) A combination of PLP and DM20 transgenes promotes partial myelination in the jimpy mouse. J Neurochem 63:822-833
    • (1994) J Neurochem , vol.63 , pp. 822-833
    • Nadon, N.L.1    Arnheiter, H.2    Hudson, L.D.3
  • 119
    • 0030900850 scopus 로고    scopus 로고
    • Aberrant protein trafficking in Trembler suggests a disease mechanism for hereditary human peripheral neuropathies
    • Naef R, Adlkofer K, Lescher B, Suter U (1997) Aberrant protein trafficking in Trembler suggests a disease mechanism for hereditary human peripheral neuropathies. Mol Cell Neurosci 9:13-25
    • (1997) Mol Cell Neurosci , vol.9 , pp. 13-25
    • Naef, R.1    Adlkofer, K.2    Lescher, B.3    Suter, U.4
  • 120
    • 0002768920 scopus 로고    scopus 로고
    • X-linked developmental defects of myelination: From mouse mutants to human genetic diseases
    • Nave KA, Boespflug-Tanguy O (1996) X-linked developmental defects of myelination: from mouse mutants to human genetic diseases. Neuroscientist 2:33-43
    • (1996) Neuroscientist , vol.2 , pp. 33-43
    • Nave, K.A.1    Boespflug-Tanguy, O.2
  • 121
    • 0023616452 scopus 로고
    • A single nucleotide difference in the gene for myelin proteolipid protein defines the jimpy mutation in mouse
    • Nave KA, Bloom FE, Milner RJ (1987) A single nucleotide difference in the gene for myelin proteolipid protein defines the jimpy mutation in mouse. Neurochem 49:1873-1877
    • (1987) Neurochem , vol.49 , pp. 1873-1877
    • Nave, K.A.1    Bloom, F.E.2    Milner, R.J.3
  • 122
    • 0022889377 scopus 로고
    • Jimpy mutant mouse: A 74-base deletion in the mRNA for myelin proteolipid protein and evidence for a primary defect in RNA splicing
    • Nave KA, Lai C, Bloom FE, Milner RJ (1986) Jimpy mutant mouse: a 74-base deletion in the mRNA for myelin proteolipid protein and evidence for a primary defect in RNA splicing. Proc Natl Acad Sci U S A 83:9264-9268
    • (1986) Proc Natl Acad Sci U S A , vol.83 , pp. 9264-9268
    • Nave, K.A.1    Lai, C.2    Bloom, F.E.3    Milner, R.J.4
  • 123
    • 0025741322 scopus 로고
    • Sodium channel density in hypomyelinated brain increased by myelin basic protein gene deletion
    • Noebels JL, Marcom PK, Jalilian-Tehrani MH (1991) Sodium channel density in hypomyelinated brain increased by myelin basic protein gene deletion. Nature 352:431-434
    • (1991) Nature , vol.352 , pp. 431-434
    • Noebels, J.L.1    Marcom, P.K.2    Jalilian-Tehrani, M.H.3
  • 124
    • 0030991166 scopus 로고    scopus 로고
    • Upregulation of the endosomal-lysosomal pathway in the trembler-J neuropathy
    • Notterpek L, Shooter EM, Snipes GJ (1997) Upregulation of the endosomal-lysosomal pathway in the trembler-J neuropathy. J Neurosci 17: 4190-4200
    • (1997) J Neurosci , vol.17 , pp. 4190-4200
    • Notterpek, L.1    Shooter, E.M.2    Snipes, G.J.3
  • 125
    • 0028231331 scopus 로고
    • Charcot-Marie-Tooth disease: A new paradigm for the mechanism of inherited disease
    • Patel PI, Lupski JR (1994) Charcot-Marie-Tooth disease: a new paradigm for the mechanism of inherited disease. Trends Genet 10:128-133
    • (1994) Trends Genet , vol.10 , pp. 128-133
    • Patel, P.I.1    Lupski, J.R.2
  • 126
    • 0027465159 scopus 로고
    • Cell-type specific interaction of Neu differentiation factor (NDF/heregulin) with Neu/HER-2 suggests complex ligand-receptor relationships
    • Peles E, Ben-Levy R, Tzahar E, Liu N, Wen D, Yarden Y (1993) Cell-type specific interaction of Neu differentiation factor (NDF/heregulin) with Neu/HER-2 suggests complex ligand-receptor relationships. EMBO J 12:961-971
    • (1993) EMBO J , vol.12 , pp. 961-971
    • Peles, E.1    Ben-Levy, R.2    Tzahar, E.3    Liu, N.4    Wen, D.5    Yarden, Y.6
  • 127
    • 0029096048 scopus 로고
    • The carbonic anhydrase domain of receptor tyrosine phosphatase beta is a functional ligand for the axonal cell recognition molecule contactin
    • Peles E, Nativ M, Campbell PL, Sakurai T, Martinez R, Lev S, Clary DO, Schilling J, Bamea G, Plowman GD, et al (1995) The carbonic anhydrase domain of receptor tyrosine phosphatase beta is a functional ligand for the axonal cell recognition molecule contactin. Cell 82:251-260
    • (1995) Cell , vol.82 , pp. 251-260
    • Peles, E.1    Nativ, M.2    Campbell, P.L.3    Sakurai, T.4    Martinez, R.5    Lev, S.6    Clary, D.O.7    Schilling, J.8    Bamea, G.9    Plowman, G.D.10
  • 129
  • 130
    • 0026132370 scopus 로고
    • Major myelin proteolipid: The 4-alpha-helix topology
    • Popot JL, Pham Dinh D, Dautigny A (1991) Major myelin proteolipid: the 4-alpha-helix topology J Membr Biol 120:233-246
    • (1991) J Membr Biol , vol.120 , pp. 233-246
    • Popot, J.L.1    Pham Dinh, D.2    Dautigny, A.3
  • 131
    • 0031963520 scopus 로고    scopus 로고
    • Peroxisomal disorders: Genotype, phenotype, major neuropathologic lesions, and pathogenesis
    • Powers JM, Moser HW (1998) Peroxisomal disorders: genotype, phenotype, major neuropathologic lesions, and pathogenesis Brain Pathol 8:101-120
    • (1998) Brain Pathol , vol.8 , pp. 101-120
    • Powers, J.M.1    Moser, H.W.2
  • 132
    • 0018333258 scopus 로고
    • Absence of the major dense line in myelin of the mutant mouse 'shiverer'
    • Privat A, Jaque C, Bourre JM, Dupouye P, Baumann N (1979) Absence of the major dense line in myelin of the mutant mouse 'shiverer'. Neurosci Lett 12:107-112
    • (1979) Neurosci Lett , vol.12 , pp. 107-112
    • Privat, A.1    Jaque, C.2    Bourre, J.M.3    Dupouye, P.4    Baumann, N.5
  • 133
    • 0024095744 scopus 로고
    • Sequence of contactin, a 130-kD glycoprotein concentrated in areas of interneuronal contact, defines a new member of the immunoglobulin supergene family in the nervous system
    • Ranscht B (1988) Sequence of contactin, a 130-kD glycoprotein concentrated in areas of interneuronal contact, defines a new member of the immunoglobulin supergene family in the nervous system. J Cell Biol 107:1561-1573
    • (1988) J Cell Biol , vol.107 , pp. 1561-1573
    • Ranscht, B.1
  • 134
    • 0026348463 scopus 로고
    • Complete deletion of the proteolipid protein gene (PLP) in a family with X-linked Pelizaeus-Merzbacher disease
    • Raskind WH, Williams CA, Hudson LD, Bird TD (1991) Complete deletion of the proteolipid protein gene (PLP) in a family with X-linked Pelizaeus-Merzbacher disease. Am J Hum Genet 49:1355-1360
    • (1991) Am J Hum Genet , vol.49 , pp. 1355-1360
    • Raskind, W.H.1    Williams, C.A.2    Hudson, L.D.3    Bird, T.D.4
  • 135
    • 0023613854 scopus 로고
    • Expression of a myelin basic protein gene in transgenic shiverer mice: Correction of the dysmyelinating phenotype
    • Readhead C, Popko B, Takahashi N, Shine HD, Saavedra RA, Sidman RL, Hood L (1987) Expression of a myelin basic protein gene in transgenic shiverer mice: correction of the dysmyelinating phenotype. Cell 48:703-712
    • (1987) Cell , vol.48 , pp. 703-712
    • Readhead, C.1    Popko, B.2    Takahashi, N.3    Shine, H.D.4    Saavedra, R.A.5    Sidman, R.L.6    Hood, L.7
  • 136
    • 0028325902 scopus 로고
    • Premature arrest of myelin formation in transgenic mice with increased dosage of the proteolipid protein gene
    • Readhead C, Schneider A, Griffiths I, Nave KA (1994) Premature arrest of myelin formation in transgenic mice with increased dosage of the proteolipid protein gene. Neuron 12:583-595
    • (1994) Neuron , vol.12 , pp. 583-595
    • Readhead, C.1    Schneider, A.2    Griffiths, I.3    Nave, K.A.4
  • 137
    • 0029962292 scopus 로고    scopus 로고
    • A recombination hotspot responsible for two inherited peripheral neuropathies is located near a mariner transposon-like element
    • Reiter LT, Murakami T, Koeuth T, Pentao L, Muzny DM, Gibbs RA, Lupski JR (1996) A recombination hotspot responsible for two inherited peripheral neuropathies is located near a mariner transposon-like element. Nature Genet 12:288-297
    • (1996) Nature Genet , vol.12 , pp. 288-297
    • Reiter, L.T.1    Murakami, T.2    Koeuth, T.3    Pentao, L.4    Muzny, D.M.5    Gibbs, R.A.6    Lupski, J.R.7
  • 139
    • 0020509790 scopus 로고
    • Characterization of cloned cDNA representing rat myelin basic protein: Absence of expression in brain of shiverer mutant mice
    • Roach A, Boylan K, Horvath S, Prusiner SB, Hood LE (1983) Characterization of cloned cDNA representing rat myelin basic protein: absence of expression in brain of shiverer mutant mice. Cell 34:799-806
    • (1983) Cell , vol.34 , pp. 799-806
    • Roach, A.1    Boylan, K.2    Horvath, S.3    Prusiner, S.B.4    Hood, L.E.5
  • 140
    • 0022413538 scopus 로고
    • Chromosomal mapping of mouse myelin basic protein gene and structure and transcription of the partially deleted gene in shiverer mutant mice
    • Roach A, Takahashi N, Pravtcheva D, Ruddle F, Hood L (1985) Chromosomal mapping of mouse myelin basic protein gene and structure and transcription of the partially deleted gene in shiverer mutant mice. Cell 42:149-155
    • (1985) Cell , vol.42 , pp. 149-155
    • Roach, A.1    Takahashi, N.2    Pravtcheva, D.3    Ruddle, F.4    Hood, L.5
  • 141
    • 0019120193 scopus 로고
    • Central myelin in the mouse mutant shiverer
    • Rosenbluth J (1980) Central myelin in the mouse mutant shiverer. J Comp Neurol 194: 639-648
    • (1980) J Comp Neurol , vol.194 , pp. 639-648
    • Rosenbluth, J.1
  • 143
  • 145
    • 0026216052 scopus 로고
    • Evolution of the myelin integral membrane proteins of the central nervous system
    • Schliess F, Stoffel W (1991) Evolution of the myelin integral membrane proteins of the central nervous system. Biol Chem Hoppe Seyler 372:865-874
    • (1991) Biol Chem Hoppe Seyler , vol.372 , pp. 865-874
    • Schliess, F.1    Stoffel, W.2
  • 146
  • 147
    • 0029079396 scopus 로고
    • Dominant-negative action of the jimpy mutation in mice complemented with an autosomal transgene for myelin proteolipid protein
    • Schneider AM, Griffiths IR, Readhead C, Nave KA (1995) Dominant-negative action of the jimpy mutation in mice complemented with an autosomal transgene for myelin proteolipid protein. Proc Natl Acad Sci USA 92:4447-4451
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 4447-4451
    • Schneider, A.M.1    Griffiths, I.R.2    Readhead, C.3    Nave, K.A.4
  • 148
    • 0023765743 scopus 로고
    • Genes specifically expressed at growth arrest of mammalian cells
    • Schneider C, King RM, Philipson L (1988) Genes specifically expressed at growth arrest of mammalian cells. Cell 54:787-793
    • (1988) Cell , vol.54 , pp. 787-793
    • Schneider, C.1    King, R.M.2    Philipson, L.3
  • 150
    • 0029145584 scopus 로고
    • Neuropathology and genetics of Pelizaeus-Merzbacher disease
    • Seitelberger F (1995) Neuropathology and genetics of Pelizaeus-Merzbacher disease. Brain Pathol 5: 267-273
    • (1995) Brain Pathol , vol.5 , pp. 267-273
    • Seitelberger, F.1
  • 152
    • 0030246987 scopus 로고    scopus 로고
    • Crystal structure of the extracellular domain from P0, the major structural protein of the peripheral nerve myelin
    • Shapiro L, Doyle JP, Hensley P, Colman DR, Hendrikson WA (1996) Crystal structure of the extracellular domain from P0, the major structural protein of the peripheral nerve myelin. Neuron 17:435-449
    • (1996) Neuron , vol.17 , pp. 435-449
    • Shapiro, L.1    Doyle, J.P.2    Hensley, P.3    Colman, D.R.4    Hendrikson, W.A.5
  • 153
    • 0026601113 scopus 로고
    • Morphometric analysis of normal, mutant, and transgenic CNS: Correlation of myelin basic protein expression to myelinogenesis
    • Shine HD, Readhead C, Popko B, Hood L, Sidman RL (1992) Morphometric analysis of normal, mutant, and transgenic CNS: correlation of myelin basic protein expression to myelinogenesis. J Neurochem. 58:342-349
    • (1992) J Neurochem. , vol.58 , pp. 342-349
    • Shine, H.D.1    Readhead, C.2    Popko, B.3    Hood, L.4    Sidman, R.L.5
  • 154
    • 37049231008 scopus 로고
    • Mutant mice (quaking and jimpy) with deficient myelination in the central nervous system
    • Sidman RL, Dickie MM, Apple SH (1964) Mutant mice (quaking and jimpy) with deficient myelination in the central nervous system. Science 144:309-311
    • (1964) Science , vol.144 , pp. 309-311
    • Sidman, R.L.1    Dickie, M.M.2    Apple, S.H.3
  • 155
    • 0028316886 scopus 로고
    • Proteolipid protein interactions in transfectants: Implications for myelin assembly
    • Sinoway MP, Kitagawa K, Timsit S, Hashim GA, Colman DR (1994) Proteolipid protein interactions in transfectants: implications for myelin assembly. J Neurosci Res 37:551-562
    • (1994) J Neurosci Res , vol.37 , pp. 551-562
    • Sinoway, M.P.1    Kitagawa, K.2    Timsit, S.3    Hashim, G.A.4    Colman, D.R.5
  • 156
    • 0030020210 scopus 로고    scopus 로고
    • A (G-to-A) mutation in the initiation codon of the proteolipid protein gene causing a relatively mild form of Pelizaeus-Merzbacher disease in a Dutch family
    • Sistermans EA, de Wijs IJ, de Coo RF, Smit LM, Menko FH, van Oost BA (1996) A (G-to-A) mutation in the initiation codon of the proteolipid protein gene causing a relatively mild form of Pelizaeus-Merzbacher disease in a Dutch family Hum Genet 97:337-339
    • (1996) Hum Genet , vol.97 , pp. 337-339
    • Sistermans, E.A.1    De Wijs, I.J.2    De Coo, R.F.3    Smit, L.M.4    Menko, F.H.5    Van Oost, B.A.6
  • 157
    • 0019979626 scopus 로고
    • Increased proliferation of oligodendrocytes in the hypomyelinated mouse mutant-jimpy
    • Skoff RP (1982) Increased proliferation of oligodendrocytes in the hypomyelinated mouse mutant-jimpy. Brain Res 248:19-31
    • (1982) Brain Res , vol.248 , pp. 19-31
    • Skoff, R.P.1
  • 158
    • 0026519132 scopus 로고
    • Characterization of a novel peripheral nervous system myelin protein (PMP-22/SR13)
    • Snipes GJ, Suter U, Welcher AA, Shooter EM (1992) Characterization of a novel peripheral nervous system myelin protein (PMP-22/SR13). J Cell Biol 117:225-238
    • (1992) J Cell Biol , vol.117 , pp. 225-238
    • Snipes, G.J.1    Suter, U.2    Welcher, A.A.3    Shooter, E.M.4
  • 159
    • 0031984825 scopus 로고    scopus 로고
    • Sox10 mutation disrupts neural crest development in Dom Hirschsprung mouse model
    • Southard-Smith EM, Kos L, Pavan WJ (1998) Sox10 mutation disrupts neural crest development in Dom Hirschsprung mouse model. Nat Genet 18:60-64
    • (1998) Nat Genet , vol.18 , pp. 60-64
    • Southard-Smith, E.M.1    Kos, L.2    Pavan, W.J.3
  • 160
    • 0024600269 scopus 로고
    • 2′,3′-cyclic nucleotide 3′-phosphodiesterase, an oligodendrocyte-Schwann cell and myelin-associated enzyme of the nervous system
    • Sprinkle TJ (1989) 2′,3′-cyclic nucleotide 3′-phosphodiesterase, an oligodendrocyte-Schwann cell and myelin-associated enzyme of the nervous system. Crit Rev Neurobiol 4:235-301
    • (1989) Crit Rev Neurobiol , vol.4 , pp. 235-301
    • Sprinkle, T.J.1
  • 161
    • 0030808781 scopus 로고    scopus 로고
    • Myelin glycolipids and their functions
    • Stoffel W, Bosio A (1997) Myelin glycolipids and their functions. Curr Opin Neurobiol 7: 654-661
    • (1997) Curr Opin Neurobiol , vol.7 , pp. 654-661
    • Stoffel, W.1    Bosio, A.2
  • 164
    • 0028851362 scopus 로고
    • Peripheral myelin protein 22: Facts and hypotheses
    • Suter U, Snipes GJ (1995a) Peripheral myelin protein 22: facts and hypotheses. J Neurosci Res 40:145-151
    • (1995) J Neurosci Res , vol.40 , pp. 145-151
    • Suter, U.1    Snipes, G.J.2
  • 165
    • 0028902548 scopus 로고
    • Biology and genetics of hereditary motor and sensory neuropathies
    • Suter U, Snipes GJ (1995b) Biology and genetics of hereditary motor and sensory neuropathies. Annu Rev Neurosci 18:45-75
    • (1995) Annu Rev Neurosci , vol.18 , pp. 45-75
    • Suter, U.1    Snipes, G.J.2
  • 166
    • 0027484361 scopus 로고
    • Perinatal lethality and defects in hindbrain development in mice homozygous for a targeted mutation of the zinc finger gene Krox20
    • Swiatek PJ, Gridley T (1993) Perinatal lethality and defects in hindbrain development in mice homozygous for a targeted mutation of the zinc finger gene Krox20. Genes Dev 11:2071-2084
    • (1993) Genes Dev , vol.11 , pp. 2071-2084
    • Swiatek, P.J.1    Gridley, T.2
  • 168
    • 0030579151 scopus 로고    scopus 로고
    • Epithelial membrane protein-2 and epithelial membrane protein-3: Two novel members of the peripheral myelin protein 22 gene family
    • Taylor V, Suter U (1996) Epithelial membrane protein-2 and epithelial membrane protein-3: two novel members of the peripheral myelin protein 22 gene family. Gene 175:115-120
    • (1996) Gene , vol.175 , pp. 115-120
    • Taylor, V.1    Suter, U.2
  • 169
    • 0031214489 scopus 로고    scopus 로고
    • Phenotypic severity of murine Plp mutants reflects in vivo and in vitro variations in transport of PLP isoproteins
    • Thomson CE, Montague P, Jung M, Nave KA, Griffiths IR (1997) Phenotypic severity of murine Plp mutants reflects in vivo and in vitro variations in transport of PLP isoproteins. Glia 20:322-332
    • (1997) Glia , vol.20 , pp. 322-332
    • Thomson, C.E.1    Montague, P.2    Jung, M.3    Nave, K.A.4    Griffiths, I.R.5
  • 176
    • 0030428795 scopus 로고    scopus 로고
    • Molecular mechanisms for Charcot-Marte-Tooth disease and related demyelinating peripheral neuropathies
    • Warner LE, Reiter LT, Murakami T, Lupski JR (1996) Molecular mechanisms for Charcot-Marte-Tooth disease and related demyelinating peripheral neuropathies. Cold Spring Harb Symp Quant Biol 61:659-671
    • (1996) Cold Spring Harb Symp Quant Biol , vol.61 , pp. 659-671
    • Warner, L.E.1    Reiter, L.T.2    Murakami, T.3    Lupski, J.R.4
  • 177
    • 0031194639 scopus 로고    scopus 로고
    • Axon-glia interactions: Building a smart nerve fiber
    • Waxman SG (1997) Axon-glia interactions: building a smart nerve fiber. Curr Biol 7:R406-R410
    • (1997) Curr Biol , vol.7
    • Waxman, S.G.1
  • 178
    • 0026980191 scopus 로고
    • Proteolipid protein (PLP) of CNS myelin: Positions of free, disulfide-bonded, and fatty acid thioester-linked cysteine residues and implications for the membrane topology of PLP
    • Weimbs T, Stoffel W (1992) Proteolipid protein (PLP) of CNS myelin: positions of free, disulfide-bonded, and fatty acid thioester-linked cysteine residues and implications for the membrane topology of PLP. Biochemistry 31:12289-12296
    • (1992) Biochemistry , vol.31 , pp. 12289-12296
    • Weimbs, T.1    Stoffel, W.2
  • 179
    • 0029149372 scopus 로고
    • Premature Schwann cell differentiation and hypermyelination in mice expressing a targeted antagonist of the POU transcription factor SCIP
    • Weinstein DE, Burrola PG, Lemke G (1995) Premature Schwann cell differentiation and hypermyelination in mice expressing a targeted antagonist of the POU transcription factor SCIP. Mol Cell Neurosci 6:212-229.
    • (1995) Mol Cell Neurosci , vol.6 , pp. 212-229
    • Weinstein, D.E.1    Burrola, P.G.2    Lemke, G.3
  • 180
    • 0027374931 scopus 로고
    • Molecular analyses of unrelated Charcot-Marie-Tooth (CMT) disease patients suggest a high frequency of the CMTIA duplication
    • Wise CA, Garcia CA, Davis SN, Heju Z, Pentao L, Patel PI, Lupski JR (1993) Molecular analyses of unrelated Charcot-Marie-Tooth (CMT) disease patients suggest a high frequency of the CMTIA duplication. Am. J. Hum. Genet 53:853-63
    • (1993) Am. J. Hum. Genet , vol.53 , pp. 853-863
    • Wise, C.A.1    Garcia, C.A.2    Davis, S.N.3    Heju, Z.4    Pentao, L.5    Patel, P.I.6    Lupski, J.R.7
  • 181
    • 0028058827 scopus 로고
    • The cytoplasmic domain of the myelin P0 protein influences the adhesive interactions of its extracellular domain
    • Wong MH, Filbin MT (1994) The cytoplasmic domain of the myelin P0 protein influences the adhesive interactions of its extracellular domain. J Cell Biol 126:1089-1097
    • (1994) J Cell Biol , vol.126 , pp. 1089-1097
    • Wong, M.H.1    Filbin, M.T.2
  • 182
    • 0029797249 scopus 로고    scopus 로고
    • Dominant-negative effect on adhesion by myelin Po protein truncated in its cytoplasmic domain
    • Wong MH, Filbin MT (1996) Dominant-negative effect on adhesion by myelin Po protein truncated in its cytoplasmic domain. J Cell Biol 134:1531-1541
    • (1996) J Cell Biol , vol.134 , pp. 1531-1541
    • Wong, M.H.1    Filbin, M.T.2
  • 183
    • 0039335177 scopus 로고    scopus 로고
    • Increased P0 glycoprotein gene dosage causes a dysmyelinating peripheral neuropathy in transgenic mice
    • Wrabetz L, Feltri M, Quattrini A, Arona M, Trapp B, Messing A (1996) Increased P0 glycoprotein gene dosage causes a dysmyelinating peripheral neuropathy in transgenic mice. Soc Neurosci Abstr 22: 1980
    • (1996) Soc Neurosci Abstr , vol.22 , pp. 1980
    • Wrabetz, L.1    Feltri, M.2    Quattrini, A.3    Arona, M.4    Trapp, B.5    Messing, A.6
  • 184
    • 0027999316 scopus 로고
    • Neuronal intermediate filaments: New progress on an old subject
    • Xu Z, Dong DL, Cleveland DW (1994) Neuronal intermediate filaments: new progress on an old subject. Curr Opin Neurobiol 4:655-661
    • (1994) Curr Opin Neurobiol , vol.4 , pp. 655-661
    • Xu, Z.1    Dong, D.L.2    Cleveland, D.W.3
  • 186
    • 0028865130 scopus 로고
    • In vivo actions of insulin-like growth factor-I (IGF-I) on brain myelination: Studies of IGF-I and IGF binding protein-1 (IGFBP-1) transgenic mice
    • Ye P, Carson J, D'Ercole AJ (1995) In vivo actions of insulin-like growth factor-I (IGF-I) on brain myelination: studies of IGF-I and IGF binding protein-1 (IGFBP-1) transgenic mice. J Neurosci 15:7344-7356
    • (1995) J Neurosci , vol.15 , pp. 7344-7356
    • Ye, P.1    Carson, J.2    D'Ercole, A.J.3
  • 187
    • 0032521342 scopus 로고    scopus 로고
    • Myelin-associated glycoprotein is a myelin signal that modulates the caliber of myelinated axons
    • Yin X, Crawford TO, Griffin JW, Tu Ph, Lee VM, Li C, Roder J, Trapp BD (1998) Myelin-associated glycoprotein is a myelin signal that modulates the caliber of myelinated axons. J Neurosci 18:1953-1962
    • (1998) J Neurosci , vol.18 , pp. 1953-1962
    • Yin, X.1    Crawford, T.O.2    Griffin, J.W.3    Tu, P.H.4    Lee, V.M.5    Li, C.6    Roder, J.7    Trapp, B.D.8
  • 188
    • 0030783521 scopus 로고    scopus 로고
    • CNP Overexpression induces aberrant oligodendrocyte membranes and inhibits MBP accumulation and myelin compaction
    • Yin X, Peterson J, Gravel M, Braun PE, Trapp BD (1997) CNP Overexpression induces aberrant oligodendrocyte membranes and inhibits MBP accumulation and myelin compaction. J. Neurosc. Res.50:238-47
    • (1997) J. Neurosc. Res. , vol.50 , pp. 238-247
    • Yin, X.1    Peterson, J.2    Gravel, M.3    Braun, P.E.4    Trapp, B.D.5
  • 189
    • 0028221758 scopus 로고
    • Elevated expression of messenger RNA for peripheral myelin protein 22 in biopsied peripheral nerves of patients with Charcot-Marie-Tooth disease type 1A
    • Yoshikawa H, Nishimura T, Nakatsuji Y, Fujimura H, Himoro M, Hayasaka K, Sakoda S, Yanagihara T (1994) Elevated expression of messenger RNA for peripheral myelin protein 22 in biopsied peripheral nerves of patients with Charcot-Marie-Tooth disease type 1A. Ann. Neurol. 35:445-450
    • (1994) Ann. Neurol. , vol.35 , pp. 445-450
    • Yoshikawa, H.1    Nishimura, T.2    Nakatsuji, Y.3    Fujimura, H.4    Himoro, M.5    Hayasaka, K.6    Sakoda, S.7    Yanagihara, T.8
  • 191
    • 0028235289 scopus 로고
    • Formation of a disulfide bond in the immunoglobulin domain of the myelin P0 protein is essential for its adhesion
    • Zhang K, Filbin MT (1994) Formation of a disulfide bond in the immunoglobulin domain of the myelin P0 protein is essential for its adhesion. J Neurochem 63:367-370
    • (1994) J Neurochem , vol.63 , pp. 367-370
    • Zhang, K.1    Filbin, M.T.2
  • 192
    • 0029810061 scopus 로고    scopus 로고
    • Mapping the adhesive domains of the myelin Po protein
    • Zhang K, Merazga Y, Filbin MT (1996) Mapping the adhesive domains of the myelin Po protein. J Neurosci Res 45:525-533
    • (1996) J Neurosci Res , vol.45 , pp. 525-533
    • Zhang, K.1    Merazga, Y.2    Filbin, M.T.3
  • 193
    • 0028950408 scopus 로고
    • Retroviral-mediated gene transfer of the peripheral myelin protein PMP22 in Schwann cells: Modulation of cell growth
    • Zoidl G, Blass-Kampmann S, D'Urso D, Schmalenbach C, Müller HW (1995) Retroviral-mediated gene transfer of the peripheral myelin protein PMP22 in Schwann cells: modulation of cell growth. EMBO J 14:1122-1128
    • (1995) EMBO J , vol.14 , pp. 1122-1128
    • Zoidl, G.1    Blass-Kampmann, S.2    D'Urso, D.3    Schmalenbach, C.4    Müller, H.W.5
  • 194
    • 0030221510 scopus 로고    scopus 로고
    • The transcription factors SCIP and Krox-20 mark distinct stages and cell fates in Schwann cell differentiation
    • Zonck TS, Syroid DE, Arroyo E, Scherer SS, Lemke G (1996) The transcription factors SCIP and Krox-20 mark distinct stages and cell fates in Schwann cell differentiation. Mol Cell Neurosci 8:129-145
    • (1996) Mol Cell Neurosci , vol.8 , pp. 129-145
    • Zonck, T.S.1    Syroid, D.E.2    Arroyo, E.3    Scherer, S.S.4    Lemke, G.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.