메뉴 건너뛰기




Volumn 52, Issue 6, 2001, Pages 656-671

Membrane traffic in myelinating oligodendrocytes

Author keywords

Disease; Membrane domains; Mistrafficking; Myelin assembly; Protein sorting; Vesicle trafficking

Indexed keywords

CELL MEMBRANES; SORTING;

EID: 0035869494     PISSN: 1059910X     EISSN: None     Source Type: Journal    
DOI: 10.1002/jemt.1050     Document Type: Review
Times cited : (83)

References (148)
  • 2
    • 0027316898 scopus 로고
    • To fold or not to fold
    • Agard DA. 1993. To fold or not to fold.. Science 260:1903-1904.
    • (1993) Science , vol.260 , pp. 1903-1904
    • Agard, D.A.1
  • 4
    • 0027367040 scopus 로고
    • Transport and localization of exogenous myelin basic protein mRNA microinjected into oligodendrocytes
    • Ainger K, Avossa D, Morgan F, Hill SJ, Barry C, Barbarese E, Carson JH. 1993. Transport and localization of exogenous myelin basic protein mRNA microinjected into oligodendrocytes. J Cell Biol 123: 431-441.
    • (1993) J Cell Biol , vol.123 , pp. 431-441
    • Ainger, K.1    Avossa, D.2    Morgan, F.3    Hill, S.J.4    Barry, C.5    Barbarese, E.6    Carson, J.H.7
  • 5
    • 0025761298 scopus 로고
    • The ectopic expression of myelin basic protein isoforms in shiverer oligodendrocytes: Implications for myelinogenesis
    • Allinquant B, Staugaitis SM, D'Urso D, Colman DR. 1991. The ectopic expression of myelin basic protein isoforms in shiverer oligodendrocytes: implications for myelinogenesis. J Cell Biol 113: 393-403.
    • (1991) J Cell Biol , vol.113 , pp. 393-403
    • Allinquant, B.1    Staugaitis, S.M.2    D'Urso, D.3    Colman, D.R.4
  • 6
    • 0034065232 scopus 로고    scopus 로고
    • On the molecular architecture of myelinated fibers
    • Arroyo EJ, Scherer SS. 2000. On the molecular architecture of myelinated fibers. Histochem Cell Biol 113:1-18.
    • (2000) Histochem Cell Biol , vol.113 , pp. 1-18
    • Arroyo, E.J.1    Scherer, S.S.2
  • 8
    • 0002440372 scopus 로고
    • Metabolism of myelin
    • Morell P, editor. New York: Plenum Press
    • Benjamins J A, Smith M. 1984. Metabolism of myelin. In: Morell P, editor. Myelin. New York: Plenum Press, pp 225-258.
    • (1984) Myelin , pp. 225-258
    • Benjamins, J.A.1    Smith, M.2
  • 9
    • 0016815002 scopus 로고
    • Appearance of newly synthesized protein in myelin of young rats
    • Benjamins JA, Jones M Morell P. 1976. Appearance of newly synthesized protein in myelin of young rats. J Neurochem 24:1117-1122.
    • (1976) J Neurochem , vol.24 , pp. 1117-1122
    • Benjamins, J.A.1    Jones, M.2    Morell, P.3
  • 11
    • 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
  • 12
    • 0033216282 scopus 로고    scopus 로고
    • Identification of a new exon in the myelin proteolipid protein gene encoding novel protein isoforms that are restricted to the somata of oligodendrocytes and neurons
    • Bongarzone ER, Campagnoni CW, Kampf K, Jacobs EC, Handley VW, Schonmann V, Campagnoni AT. 1999. Identification of a new exon in the myelin proteolipid protein gene encoding novel protein isoforms that are restricted to the somata of oligodendrocytes and neurons.J Neurosci 19:8349-8357.
    • (1999) J Neurosci , vol.19 , pp. 8349-8357
    • Bongarzone, E.R.1    Campagnoni, C.W.2    Kampf, K.3    Jacobs, E.C.4    Handley, V.W.5    Schonmann, V.6    Campagnoni, A.T.7
  • 13
    • 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, Bincek 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    Bincek, E.2    Stoffel, W.3
  • 14
    • 0034141404 scopus 로고    scopus 로고
    • Expression of rab GTP-binding proteins during oligodendrocyte differentiation in culture
    • Bouverat BP, Krüger WH, Coetzee T, Bansal R, Pfeiffer SE. 2000. Expression of rab GTP-binding proteins during oligodendrocyte differentiation in culture. J Neurosci Res 59:446-543.
    • (2000) J Neurosci Res , vol.59 , pp. 446-543
    • Bouverat, B.P.1    Krüger, W.H.2    Coetzee, T.3    Bansal, R.4    Pfeiffer, S.E.5
  • 15
    • 0032516859 scopus 로고    scopus 로고
    • Membrane traffic in polarized neurons
    • Bradke F, Dotti CG. 1998. Membrane traffic in polarized neurons. Biochim Biophys Acta 1404:245-258.
    • (1998) Biochim Biophys Acta , vol.1404 , pp. 245-258
    • Bradke, F.1    Dotti, C.G.2
  • 16
    • 0025285449 scopus 로고
    • Identification of GTP-binding proteins in myelin and oligodendrocyte membranes
    • Braun PE, Horvath E, Yong VW, Bernier L. 1990. Identification of GTP-binding proteins in myelin and oligodendrocyte membranes. J Neurosci Res 26:16-23.
    • (1990) J Neurosci Res , vol.26 , pp. 16-23
    • Braun, P.E.1    Horvath, E.2    Yong, V.W.3    Bernier, L.4
  • 17
    • 0023787396 scopus 로고
    • Immunocytochemical localization by electron microscopy of 2′3′-cyclic nucleotide 3′-phosphodiesterase in developing oligodendrocytes of normal and mutant brain
    • Braun PE, Sandillon F, Edwards A, Matthieu JM, Privat A. 1988. Immunocytochemical localization by electron microscopy of 2′3′-cyclic nucleotide 3′-phosphodiesterase in developing oligodendrocytes of normal and mutant brain. J Neurosci 8:3057-3066.
    • (1988) J Neurosci , vol.8 , pp. 3057-3066
    • Braun, P.E.1    Sandillon, F.2    Edwards, A.3    Matthieu, J.M.4    Privat, A.5
  • 18
    • 0034653108 scopus 로고    scopus 로고
    • Involvement of OSP/claudin-11 in oligodendrocyte membrane interactions: Role in biology and disease
    • Bronstein JM, Tiwari-Woodruff S, Buznikov AG, Stevens DB. 2000. Involvement of OSP/claudin-11 in oligodendrocyte membrane interactions: role in biology and disease. J Neurosci Res 59:706-711.
    • (2000) J Neurosci Res , vol.59 , pp. 706-711
    • Bronstein, J.M.1    Tiwari-Woodruff, S.2    Buznikov, A.G.3    Stevens, D.B.4
  • 19
    • 0027493309 scopus 로고
    • The distribution of myelin basic protein mRNAs within myelinating oligodendrocytes
    • Brophy PJ, Boccaccio GL, Coleman DR. 1993. The distribution of myelin basic protein mRNAs within myelinating oligodendrocytes. Trends Neurosci 16:515-521.
    • (1993) Trends Neurosci , vol.16 , pp. 515-521
    • Brophy, P.J.1    Boccaccio, G.L.2    Coleman, D.R.3
  • 20
    • 0032421354 scopus 로고    scopus 로고
    • Functions of lipid rafts in biological membranes
    • Brown DA, London E. 1998. Functions of lipid rafts in biological membranes. Annu Rev Cell Dev Biol 14:111-136.
    • (1998) Annu Rev Cell Dev Biol , vol.14 , pp. 111-136
    • Brown, D.A.1    London, E.2
  • 21
    • 0034625373 scopus 로고    scopus 로고
    • Structure and function of sphingolipid-and cholesterol-rich membrane rafts
    • Brown DA, London E. 2000. Structure and function of sphingolipid-and cholesterol-rich membrane rafts. J Biol Chem 275:17221-17224.
    • (2000) J Biol Chem , vol.275 , pp. 17221-17224
    • Brown, D.A.1    London, E.2
  • 23
    • 0031965054 scopus 로고    scopus 로고
    • Sphingolipid organization in biomembranes: What physical studies of model membranes reveal
    • Brown RE. 1998. Sphingolipid organization in biomembranes: what physical studies of model membranes reveal. J Cell Sci 111:1-9.
    • (1998) J Cell Sci , vol.111 , pp. 1-9
    • Brown, R.E.1
  • 24
    • 0024535322 scopus 로고
    • Differential ultrastructural localization of myelin basic protein, myelin/oligodendroglial glycoprotein, and 2′,3′-cyclic nucleotide 3′-phosphodiesterase in the CNS of adult rats
    • Brunner C, Lassmann H, Waehneldt TV, Matthieu JM, Linington C. 1989. Differential ultrastructural localization of myelin basic protein, myelin/oligodendroglial glycoprotein, and 2′,3′-cyclic nucleotide 3′-phosphodiesterase in the CNS of adult rats. J Neurochem 52:296-304.
    • (1989) J Neurochem , vol.52 , pp. 296-304
    • Brunner, C.1    Lassmann, H.2    Waehneldt, T.V.3    Matthieu, J.M.4    Linington, C.5
  • 28
    • 0001619084 scopus 로고    scopus 로고
    • VIP17/ MAL, a lipid raft-associated protein, is involved in apical transport in MDCK cells
    • Cheong KH, Zacchetti D, Schneeberger EE, Simons K. 1999. VIP17/ MAL, a lipid raft-associated protein, is involved in apical transport in MDCK cells. Proc Natl Acad Sci USA 96:6241-6248.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 6241-6248
    • Cheong, K.H.1    Zacchetti, D.2    Schneeberger, E.E.3    Simons, K.4
  • 29
    • 0033571899 scopus 로고    scopus 로고
    • Subcellular localization of tetanus neurotoxin-insensitive vesicle-associated membrane protein (VAMP)/ VAMP7 in neuronal cells: Evidence for a novel membrane compartment
    • Coco S, Raposo G, Martinez S, Fontaine JJ, Takamori S, Zahraoui A, Jahn R, Matteoli M, Louvard D, Galli T. 1999. Subcellular localization of tetanus neurotoxin-insensitive vesicle-associated membrane protein (VAMP)/ VAMP7 in neuronal cells: evidence for a novel membrane compartment. J Neurosci 19:9803-9812.
    • (1999) J Neurosci , vol.19 , pp. 9803-9812
    • Coco, S.1    Raposo, G.2    Martinez, S.3    Fontaine, J.J.4    Takamori, S.5    Zahraoui, A.6    Jahn, R.7    Matteoli, M.8    Louvard, D.9    Galli, T.10
  • 30
    • 0032781971 scopus 로고    scopus 로고
    • Myelination in the absence of galactolipids and proteolipid proteins
    • Coetzee T, Suzuki K, Nave KA, Popko B. 1999. Myelination in the absence of galactolipids and proteolipid proteins. Mol Cell Neurosci 14:41-51.
    • (1999) Mol Cell Neurosci , vol.14 , pp. 41-51
    • Coetzee, T.1    Suzuki, K.2    Nave, K.A.3    Popko, B.4
  • 31
    • 0030602822 scopus 로고    scopus 로고
    • Myelination in the absence of galactocerebroside and sulfatide: Normal structure with abnormal function and regional instability
    • Coetzee T, Fujita Nn, 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, Nn.2    Dupree, J.3    Shi, R.4    Blight, A.5    Suzuki, K.6    Suzuki, K.7    Popko, B.8
  • 32
    • 0020372097 scopus 로고
    • Synthesis and incorporation of myelin polypeptides into CNS myelin
    • Coleman DR, Kreibich G, Frey AB, Sabatini DD. 1982. Synthesis and incorporation of myelin polypeptides into CNS myelin. J Cell Biol 95:598-608.
    • (1982) J Cell Biol , vol.95 , pp. 598-608
    • Coleman, D.R.1    Kreibich, G.2    Frey, A.B.3    Sabatini, D.D.4
  • 33
    • 0029123983 scopus 로고
    • Virus entry and release in polarized epithelial cells
    • Compans RW. 1995. Virus entry and release in polarized epithelial cells. Curr Top Microbiol Immunol 202:209-219
    • (1995) Curr Top Microbiol Immunol , vol.202 , pp. 209-219
    • Compans, R.W.1
  • 35
    • 0031050896 scopus 로고    scopus 로고
    • Differential and cell development-dependent localization of myelin mRNAs in oligodendrocytes
    • deVries H, deJonge JC, Schrage C, van der Haar ME, Hoeckstra D. 1997. Differential and cell development-dependent localization of myelin mRNAs in oligodendrocytes. J Neurosci Res 47:479-488.
    • (1997) J Neurosci Res , vol.47 , pp. 479-488
    • DeVries, H.1    DeJonge, J.C.2    Schrage, C.3    Van Der Haar, M.E.4    Hoeckstra, D.5
  • 36
    • 0031918326 scopus 로고    scopus 로고
    • An apical-type trafficking pathway is present in cultured oligodendrocytes but the sphingo-lipid-enriched myelin membrane is the target of a basolateral-type pathway
    • deVries H, Schrage C, Hoeckstra D. 1998. An apical-type trafficking pathway is present in cultured oligodendrocytes but the sphingo-lipid-enriched myelin membrane is the target of a basolateral-type pathway. Mol Biol Cell 9:599-609.
    • (1998) Mol Biol Cell , vol.9 , pp. 599-609
    • DeVries, H.1    Schrage, C.2    Hoeckstra, D.3
  • 37
    • 0026580004 scopus 로고
    • Local modulation of neurofilament phosphorylation, axonal caliber, and slow axonal transport by myelinating Schwann cells
    • deWaegh SM, Lee VM, Brady ST. 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.M.1    Lee, V.M.2    Brady, S.T.3
  • 38
    • 0022590780 scopus 로고
    • Emergence of three myelin proteins in oligodendrocytes cultured without neurons
    • Dubois-Dalcq M, Behar T, Hudson L, Lazzarini RA. 1986. Emergence of three myelin proteins in oligodendrocytes cultured without neurons. J Cell Biol 102:384-392.
    • (1986) J Cell Biol , vol.102 , pp. 384-392
    • Dubois-Dalcq, M.1    Behar, T.2    Hudson, L.3    Lazzarini, R.A.4
  • 39
    • 0031972929 scopus 로고    scopus 로고
    • Overloaded endoplasmic reticulum-Golgi 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, Müller HW. 1998. Overloaded endoplasmic reticulum-Golgi 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    Müller, H.W.5
  • 40
    • 0028827606 scopus 로고
    • Myelin-associated glycoprotein: A role in myelination and in the inhibition of axonal regeneration?
    • Filbin MT. 1995. Myelin-associated glycoprotein: a role in myelination and in the inhibition of axonal regeneration? Curr Opin Neurobiol 5:588-595.
    • (1995) Curr Opin Neurobiol , vol.5 , pp. 588-595
    • Filbin, M.T.1
  • 41
    • 0033964123 scopus 로고    scopus 로고
    • MAL, a proteolipid in glycosphingolipid enriched domains: Functional implications in myelin and beyond
    • Frank M. 2000. MAL, a proteolipid in glycosphingolipid enriched domains: functional implications in myelin and beyond. Prog Neurobiol 60:531-544.
    • (2000) Prog Neurobiol , vol.60 , pp. 531-544
    • Frank, M.1
  • 42
    • 0032124916 scopus 로고    scopus 로고
    • rMAL is a glycosphingolipid-associated protein of myelin and apical membranes of epithelial cells in kidney and stomach
    • Frank M, van der Haar ME, Schaeren-Wiemers N, Schwab ME. 1998. rMAL is a glycosphingolipid-associated protein of myelin and apical membranes of epithelial cells in kidney and stomach. J Neurosci 18:4901-4913.
    • (1998) J Neurosci , vol.18 , pp. 4901-4913
    • Frank, M.1    Van Der Haar, M.E.2    Schaeren-Wiemers, N.3    Schwab, M.E.4
  • 44
    • 0031814298 scopus 로고    scopus 로고
    • A novel tetanus neurotoxin-insensitive vesicle-associated membrane protein in SNARE complexes of the apical plasma membrane of epithelial cells
    • Galli T, Zahraoui A, Vaidyanathan W, Raposo G, Tian JM, Karin M, Niemann H, Louvard D. 1998. A novel tetanus neurotoxin-insensitive vesicle-associated membrane protein in SNARE complexes of the apical plasma membrane of epithelial cells. Mol Biol Cell 9:1437-1448.
    • (1998) Mol Biol Cell , vol.9 , pp. 1437-1448
    • Galli, T.1    Zahraoui, A.2    Vaidyanathan, W.3    Raposo, G.4    Tian, J.M.5    Karin, M.6    Niemann, H.7    Louvard, D.8
  • 45
    • 0030821122 scopus 로고    scopus 로고
    • Oligodendrocytes express different isoforms of β-amyloid precursor protein in chemically defined cell culture conditions: In situ hybridization and immunocytochemical detection
    • Garcia-Ladona FJ, Huss Y, Frey P, Ghandour MS. 1997. Oligodendrocytes express different isoforms of β-amyloid precursor protein in chemically defined cell culture conditions: in situ hybridization and immunocytochemical detection. J Neurosci Res 50:50-61.
    • (1997) J Neurosci Res , vol.50 , pp. 50-61
    • Garcia-Ladona, F.J.1    Huss, Y.2    Frey, P.3    Ghandour, M.S.4
  • 46
    • 0344466781 scopus 로고    scopus 로고
    • Characterization and Dynamics of Aggresome Formation by a Cytosolic GFP-Chimera
    • García-Mata R, Bebök Z, Sorscher EJ, Sztul ES. 1999. Characterization and Dynamics of Aggresome Formation by a Cytosolic GFP-Chimera. J Cell Biol 146:1239-1254.
    • (1999) J Cell Biol , vol.146 , pp. 1239-1254
    • García-Mata, R.1    Bebök, Z.2    Sorscher, E.J.3    Sztul, E.S.4
  • 47
    • 0027639966 scopus 로고
    • The modification and assembly of proteins in the endoplasmic reticulum
    • Gaut JR, Hendershot LM. 1993. The modification and assembly of proteins in the endoplasmic reticulum. Curr Opin Cell Biol 5:589-595.
    • (1993) Curr Opin Cell Biol , vol.5 , pp. 589-595
    • Gaut, J.R.1    Hendershot, L.M.2
  • 48
    • 0026060227 scopus 로고
    • In situ hybridization analysis of mRNAs for carbonic anhydrase II and myelin basic protein: Expression in developing cultured glial cells
    • Ghandour MS, Skoff RP. 1991. In situ hybridization analysis of mRNAs for carbonic anhydrase II and myelin basic protein: expression in developing cultured glial cells. Glia 4:1-10.
    • (1991) Glia , vol.4 , pp. 1-10
    • Ghandour, M.S.1    Skoff, R.P.2
  • 49
    • 0033582905 scopus 로고    scopus 로고
    • Regulation of membrane trafficking: Structural insights from a Rah/effector complex
    • Gonzalez L Jr, Scheller R H. 1999. Regulation of membrane trafficking: Structural insights from a Rah/effector complex. Cell 96:755-758.
    • (1999) Cell , vol.96 , pp. 755-758
    • Gonzalez Jr., L.1    Scheller, R.H.2
  • 50
    • 0032717797 scopus 로고    scopus 로고
    • Myelin-associated oligodendrocytic basic protein mRNAs reside at different subcellular locations
    • Gould RM, Freund CM, Barbarese E. 1999. Myelin-associated oligodendrocytic basic protein mRNAs reside at different subcellular locations. J Neurochem 73:1913-24.
    • (1999) J Neurochem , vol.73 , pp. 1913-1924
    • Gould, R.M.1    Freund, C.M.2    Barbarese, E.3
  • 51
    • 0028226949 scopus 로고
    • Many naturally occuring mutations of myelin proteolipid protein impair its intracellular transport
    • Gow A, Friedrich VL, Lazzarini RA. 1994b. Many naturally occuring 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
  • 52
    • 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. Nature Gen 13:422-428.
    • (1996) Nature Gen , vol.13 , pp. 422-428
    • Gow, A.1    Lazzarini, R.A.2
  • 53
    • 0028287054 scopus 로고
    • Intracellular transport and sorting of the oligodendrocyte transmembrane proteolipid protein
    • Gow A, Friedrich VL, Lazzarini RA. 1994a. Intracellular transport and sorting of the oligodendrocyte transmembrane proteolipid protein. J Neurosci Res 37:563-573.
    • (1994) J Neurosci Res , vol.37 , pp. 563-573
    • Gow, A.1    Friedrich, V.L.2    Lazzarini, R.A.3
  • 54
    • 0032559544 scopus 로고    scopus 로고
    • Disrupted proteolipid trafficking results in oligodendrocyte apoptosis in an animal model of Pelizaeus-Merzbacher disease
    • Gow A, Southwood CM, Lazzarini RA. 1998. Disrupted proteolipid 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
  • 56
    • 0026934552 scopus 로고
    • Cell biology of viruses that assemble along the biosynthetic pathway
    • Griffiths G, Rottier P. 1992. Cell biology of viruses that assemble along the biosynthetic pathway. Semin Cell Biol 3:367-381.
    • (1992) Semin Cell Biol , vol.3 , pp. 367-381
    • Griffiths, G.1    Rottier, P.2
  • 59
    • 0030796026 scopus 로고    scopus 로고
    • SNAREs and NSF in targeted membrane fusion
    • Hay JC, Scheller R. 1997. SNAREs and NSF in targeted membrane fusion. Curr Opin Cell Biol 9:505-512.
    • (1997) Curr Opin Cell Biol , vol.9 , pp. 505-512
    • Hay, J.C.1    Scheller, R.2
  • 60
    • 0030684039 scopus 로고    scopus 로고
    • Dendroaxonal transcytosis of transferrin in cultured hippocampal and sympathetic neurons
    • Hemar A, Olivo JC, Williamson E, Saffrich R, Dotti CG. 1997. Dendroaxonal transcytosis of transferrin in cultured hippocampal and sympathetic neurons. J Neurosci 17:9026-9034
    • (1997) J Neurosci , vol.17 , pp. 9026-9034
    • Hemar, A.1    Olivo, J.C.2    Williamson, E.3    Saffrich, R.4    Dotti, C.G.5
  • 62
    • 0030058663 scopus 로고    scopus 로고
    • Molecular and developmental characterization of novel cDNAs of the myelin-associated oligodendrocytic basic protein
    • Holz A, Schaeren-Wiemers N, Schaefer C, Pott U, Collelo RJ, Schwab ME. 1996. Molecular and developmental characterization of novel cDNAs of the myelin-associated oligodendrocytic basic protein. J Neurochem 16:467-477.
    • (1996) J Neurochem , vol.16 , pp. 467-477
    • Holz, A.1    Schaeren-Wiemers, N.2    Schaefer, C.3    Pott, U.4    Collelo, R.J.5    Schwab, M.E.6
  • 63
    • 0028353055 scopus 로고
    • Myelin membrane biogenesis by oligodendrocytes. Developmental regulation of low molecular weight GTP-binding proteins
    • Huber LA, Madison DL, Simons K, Pfeiffer SE. 1994. Myelin membrane biogenesis by oligodendrocytes. Developmental regulation of low molecular weight GTP-binding proteins. FEBS Letters 347: 273-278.
    • (1994) FEBS Letters , vol.347 , pp. 273-278
    • Huber, L.A.1    Madison, D.L.2    Simons, K.3    Pfeiffer, S.E.4
  • 64
    • 0024394494 scopus 로고
    • The initial events in myelin synthesis: Orientation of proteolipid protein in the plasmamembrane of cultured oligodendrocytes
    • Hudson LD, Friedrich VL, Behar T, Dubois-Dalcq M, Lazzarini RA. 1989. The initial events in myelin synthesis: orientation of proteolipid protein in the plasmamembrane of cultured oligodendrocytes. J Cell Biol 109:717-727.
    • (1989) J Cell Biol , vol.109 , pp. 717-727
    • Hudson, L.D.1    Friedrich, V.L.2    Behar, T.3    Dubois-Dalcq, M.4    Lazzarini, R.A.5
  • 66
    • 0028216869 scopus 로고
    • Synaptic vesicles and exocytosis
    • Jahn R, Südhof TC. 1994. Synaptic vesicles and exocytosis. Annu Rev Neurosci 17:219-246.
    • (1994) Annu Rev Neurosci , vol.17 , pp. 219-246
    • Jahn, R.1    Südhof, T.C.2
  • 67
    • 0032836484 scopus 로고    scopus 로고
    • Membrane fusion and exocytosis
    • Jahn R, Südhof TC. 1999. Membrane fusion and exocytosis. Annu Rev Biochem 68:863-911.
    • (1999) Annu Rev Biochem , vol.68 , pp. 863-911
    • Jahn, R.1    Südhof, T.C.2
  • 68
    • 0032576605 scopus 로고    scopus 로고
    • Aggresomes: A cellular response to misfolded proteins
    • Johnston JA, Ward CL, Kopito RR. 1998. Aggresomes: a cellular response to misfolded proteins J. Cell Biol 143:1883-1898
    • (1998) J. Cell Biol , vol.143 , pp. 1883-1898
    • Johnston, J.A.1    Ward, C.L.2    Kopito, R.R.3
  • 70
    • 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
  • 71
    • 0033400053 scopus 로고    scopus 로고
    • Inherited peripheral neuropathy
    • Keller MP, Chance PF. 1999. Inherited peripheral neuropathy. Semin Neurol 19:353-362
    • (1999) Semin Neurol , vol.19 , pp. 353-362
    • Keller, M.P.1    Chance, P.F.2
  • 72
    • 0033497984 scopus 로고    scopus 로고
    • Myelin glycosphingolipid/cholesterol-enriched microdomains selectively sequester the non-compact myelin proteins CNP and MOG
    • Kim T, Pfeiffer SE. 1999. Myelin glycosphingolipid/cholesterol-enriched microdomains selectively sequester the non-compact myelin proteins CNP and MOG. J Neurocytol 28:281-293.
    • (1999) J Neurocytol , vol.28 , pp. 281-293
    • Kim, T.1    Pfeiffer, S.E.2
  • 73
    • 0028875824 scopus 로고
    • Cloning and characterization of MVP17: A developmentally regulated myelin protein in oligodendrocytes
    • Kim T, Fiedler K, Madison DL, Krueger WH, Pfeiffer SE. 1995. Cloning and characterization of MVP17: A developmentally regulated myelin protein in oligodendrocytes. J Neurosci Res 42: 413-422.
    • (1995) J Neurosci Res , vol.42 , pp. 413-422
    • Kim, T.1    Fiedler, K.2    Madison, D.L.3    Krueger, W.H.4    Pfeiffer, S.E.5
  • 75
    • 0022540450 scopus 로고
    • Oligodendroglial cell death in jimpy mice: An explanation for the myelin deficit
    • Knapp PE, Skoff RP, Redstone DW. 1986. Oligodendroglial cell death in jimpy mice: An explanation for the myelin deficit. J Neurosci 6:2813-2822.
    • (1986) J Neurosci , vol.6 , pp. 2813-2822
    • Knapp, P.E.1    Skoff, R.P.2    Redstone, D.W.3
  • 76
    • 0344053287 scopus 로고    scopus 로고
    • Oligodendrocytes direct glycosyl phosphatidylinositol-anchored proteins to the myelin sheath in glycosphingolipid-rich complexes
    • Krämer EM, Koch T, Niehaus A, Trotter J. 1997. Oligodendrocytes direct glycosyl phosphatidylinositol-anchored proteins to the myelin sheath in glycosphingolipid-rich complexes. J Biol Chem 272:8937-8945.
    • (1997) J Biol Chem , vol.272 , pp. 8937-8945
    • Krämer, E.M.1    Koch, T.2    Niehaus, A.3    Trotter, J.4
  • 77
    • 0038933866 scopus 로고    scopus 로고
    • Compartmentation of Fyn kinase with glycosylphosphatidylinositol-anchored molecules in oligodendrocytes facilitates kinaase activation during myelination
    • Krämer EM, Klein C, Koch T, Boytinck M, Trotter J. 1999. Compartmentation of Fyn kinase with glycosylphosphatidylinositol-anchored molecules in oligodendrocytes facilitates kinaase activation during myelination. J Biol Chem 274:29042-29049.
    • (1999) J Biol Chem , vol.274 , pp. 29042-29049
    • Krämer, E.M.1    Klein, C.2    Koch, T.3    Boytinck, M.4    Trotter, J.5
  • 78
    • 0033616708 scopus 로고    scopus 로고
    • Raft association of SNAP receptors acting in apical trafficking in Madi-Darby canine kidney cells
    • Lafont F, Verkade P, Galli T, Wimmer C, Louvard D, Simons K. 1999. Raft association of SNAP receptors acting in apical trafficking in Madi-Darby canine kidney cells. Proc Natl Acad Sci USA 96: 3734-3738.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 3734-3738
    • Lafont, F.1    Verkade, P.2    Galli, T.3    Wimmer, C.4    Louvard, D.5    Simons, K.6
  • 79
    • 0034051162 scopus 로고    scopus 로고
    • Membrane rafts and signaling by the multichain immune recognition receptors
    • Langlet C, Bernard AM, Drevot P, He HT. 2000. Membrane rafts and signaling by the multichain immune recognition receptors. Curr Opin Immunol 12:250-255.
    • (2000) Curr Opin Immunol , vol.12 , pp. 250-255
    • Langlet, C.1    Bernard, A.M.2    Drevot, P.3    He, H.T.4
  • 80
    • 0026075048 scopus 로고
    • Detection of G proteins in purified bovine brain myelin
    • Larocca JN, Golly F, Ledeen RW. 1991. Detection of G proteins in purified bovine brain myelin. J Neurochem 57:30-38.
    • (1991) J Neurochem , vol.57 , pp. 30-38
    • Larocca, J.N.1    Golly, F.2    Ledeen, R.W.3
  • 81
    • 0345130002 scopus 로고    scopus 로고
    • Maturation of the axonal plasma membrane requires upregulation of sphingomyelin synthesis and formation of protein-lipid complexes
    • Ledesma MD, Brugger B, Sunning FT, Wieland FT, Dotti CG. 1999. Maturation of the axonal plasma membrane requires upregulation of sphingomyelin synthesis and formation of protein-lipid complexes. EMBO J 18:1761-1771.
    • (1999) EMBO J , vol.18 , pp. 1761-1771
    • Ledesma, M.D.1    Brugger, B.2    Sunning, F.T.3    Wieland, F.T.4    Dotti, C.G.5
  • 82
    • 0000029565 scopus 로고
    • Proteins of myelin
    • Morell P, editor. New York: Plenum Press
    • Lees MB, Brostoff SW. 1984. Proteins of myelin. In: Morell P, editor. Myelin. New York: Plenum Press, p 197-217.
    • (1984) Myelin , pp. 197-217
    • Lees, M.B.1    Brostoff, S.W.2
  • 83
    • 0031051488 scopus 로고    scopus 로고
    • Connexin32 in oligodendrocytes and association with myelinated fibers in mouse and rat brain
    • Li J, Hertzberg EL, Nagy JI. 1997. Connexin32 in oligodendrocytes and association with myelinated fibers in mouse and rat brain. J Comp Neurol 379:571-591.
    • (1997) J Comp Neurol , vol.379 , pp. 571-591
    • Li, J.1    Hertzberg, E.L.2    Nagy, J.I.3
  • 84
    • 0028853922 scopus 로고
    • Functional implications for the microtubule-associated protein tau: Localization in oligodendrocytes
    • LoPresti P, Szuchet S, Papasozomenos SC, Zinkowski RP, Binder LI. 1995. Functional implications for the microtubule-associated protein tau: localization in oligodendrocytes. Proc Nat Acad Sci USA 92:10369-10373.
    • (1995) Proc Nat Acad Sci USA , vol.92 , pp. 10369-10373
    • LoPresti, P.1    Szuchet, S.2    Papasozomenos, S.C.3    Zinkowski, R.P.4    Binder, L.I.5
  • 85
  • 89
    • 0005826964 scopus 로고    scopus 로고
    • Do secretory pathway SNARE proteins mediate myelinogenesis?
    • Juurlink et al., eds. New York: Plenum Press
    • Madison DE, Pfeiffer SE. 1997. Do secretory pathway SNARE proteins mediate myelinogenesis? In: Juurlink et al., eds. Cell biology and pathology of myelin. New York: Plenum Press, p 145-154.
    • (1997) Cell Biology and Pathology of Myelin , pp. 145-154
    • Madison, D.E.1    Pfeiffer, S.E.2
  • 90
    • 0033009470 scopus 로고    scopus 로고
    • SNARE complex proteins, including the cognate pair VAMP-2 and syntaxin-4 are expressed in cultured oligodendrocytes
    • Madison DL, Krueger WH, Cheng D, Trapp BD, Pfeiffer SE. 1999. SNARE complex proteins, including the cognate pair VAMP-2 and syntaxin-4 are expressed in cultured oligodendrocytes. J Neurochem 72:988-998.
    • (1999) J Neurochem , vol.72 , pp. 988-998
    • Madison, D.L.1    Krueger, W.H.2    Cheng, D.3    Trapp, B.D.4    Pfeiffer, S.E.5
  • 91
    • 0029768928 scopus 로고    scopus 로고
    • Differential expression of rab3 isoforms in oligodendrocytes and astrocytes
    • Madison DL, Krüger WH, Kim T, Pfeiffer SE. 1996. Differential expression of rab3 isoforms in oligodendrocytes and astrocytes. J Neurosci Res 45:258-268.
    • (1996) J Neurosci Res , vol.45 , pp. 258-268
    • Madison, D.L.1    Krüger, W.H.2    Kim, T.3    Pfeiffer, S.E.4
  • 92
    • 0034614647 scopus 로고    scopus 로고
    • The road taken: Past and future foundations of membrane traffic
    • Mellman I, Warren G. 2000. The road taken: past and future foundations of membrane traffic. Cell 100:99-112.
    • (2000) Cell , vol.100 , pp. 99-112
    • Mellman, I.1    Warren, G.2
  • 93
    • 0029950852 scopus 로고    scopus 로고
    • Differential intracellular sorting of the myelin-associated glycoprotein isoforms
    • Minuk J, Braun PE. 1996. Differential intracellular sorting of the myelin-associated glycoprotein isoforms. J Neurosci Res 44:411-420.
    • (1996) J Neurosci Res , vol.44 , pp. 411-420
    • Minuk, J.1    Braun, P.E.2
  • 94
    • 0032145173 scopus 로고    scopus 로고
    • Protein toxins and membrane transport
    • Montecucco C. 1998. Protein toxins and membrane transport. Curr Opin Cell Biol 10:530-536.
    • (1998) Curr Opin Cell Biol , vol.10 , pp. 530-536
    • Montecucco, C.1
  • 95
    • 0033519348 scopus 로고    scopus 로고
    • Claudin-11/OSP-based tight junctions of myelin sheaths in brain and Sertoli cells in testis
    • Monta K, Sasaki H, Fujimoto K, Furuse M, Tsukita S. 1999. Claudin-11/OSP-based tight junctions of myelin sheaths in brain and Sertoli cells in testis. J Cell Biol 145:579-588.
    • (1999) J Cell Biol , vol.145 , pp. 579-588
    • Monta, K.1    Sasaki, H.2    Fujimoto, K.3    Furuse, M.4    Tsukita, S.5
  • 96
    • 0029240448 scopus 로고
    • Regulation of protein traffic in polarized epithelial cells
    • Mostov KE, Cardone MH. 1995. Regulation of protein traffic in polarized epithelial cells. BioEssays 17:129-138.
    • (1995) BioEssays , vol.17 , pp. 129-138
    • Mostov, K.E.1    Cardone, M.H.2
  • 98
    • 17444451522 scopus 로고    scopus 로고
    • Tetraspan myelin protein PMP22 and demyelinating peripheral neuropathies: New facts and hypotheses
    • Müller HW. 2000. Tetraspan myelin protein PMP22 and demyelinating peripheral neuropathies: new facts and hypotheses. Glia 29: 182-185.
    • (2000) Glia , vol.29 , pp. 182-185
    • Müller, H.W.1
  • 99
    • 0030900850 scopus 로고    scopus 로고
    • Abberant protein trafficking in Trembler suggests a disease mechanism for hereditary human peripheral neuropathies
    • Naef R, Adlkofer K, Lescher B, Suter U. 1997. Abberant 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
  • 100
    • 0032894049 scopus 로고    scopus 로고
    • Impaired intracellular trafficking is a common disease mechanism of PMP22 point mutations in peripheral neuropathies
    • Naef R, Suter U. 1999. Impaired intracellular trafficking is a common disease mechanism of PMP22 point mutations in peripheral neuropathies. Neurobiol Dis 6:1-14.
    • (1999) Neurobiol Dis , vol.6 , pp. 1-14
    • Naef, R.1    Suter, U.2
  • 101
    • 0023389399 scopus 로고
    • Splice site selection in the proteolipid protein (PLP) gene transcript and primary structure of the DM-20 protein of central nervous system myelin
    • Nave KA, Lai C, Bloom FE, Milner RJ. 1987. Splice site selection in the proteolipid protein (PLP) gene transcript and primary structure of the DM-20 protein of central nervous system myelin. Proc Natl Acad Sci USA 84:5665-5669.
    • (1987) Proc Natl Acad Sci USA , vol.84 , pp. 5665-5669
    • Nave, K.A.1    Lai, C.2    Bloom, F.E.3    Milner, R.J.4
  • 102
    • 0030722286 scopus 로고    scopus 로고
    • Expression of molecular chaperones and vesicle transport proteins in differentiating oligodendrocytes
    • Neri CL, Duchala CS, Macklin WB. 1997. Expression of molecular chaperones and vesicle transport proteins in differentiating oligodendrocytes. J Neurisci Res 50:769-780.
    • (1997) J Neurisci Res , vol.50 , pp. 769-780
    • Neri, C.L.1    Duchala, C.S.2    Macklin, W.B.3
  • 104
    • 0000072448 scopus 로고
    • Isolation and characterization of myelin
    • Morell P, editor. New York: Plenum Press
    • Norton WT, Cammer W. 1984. Isolation and characterization of myelin. In: Morell P, editor. Myelin. New York: Plenum Press, p 147-195.
    • (1984) Myelin , pp. 147-195
    • Norton, W.T.1    Cammer, W.2
  • 105
    • 0030860083 scopus 로고    scopus 로고
    • The diversity of Rab proteins in vesicle transport
    • Novick P, Zerial M. 1997. The diversity of Rab proteins in vesicle transport. Curr Opin Cell Biol 9:496-504.
    • (1997) Curr Opin Cell Biol , vol.9 , pp. 496-504
    • Novick, P.1    Zerial, M.2
  • 106
    • 0021088280 scopus 로고
    • Immunocytochemical demonstration of the transport of myelin proteins through the golgi apparatus
    • Nussbaum JL, Roussel G. 1983. Immunocytochemical demonstration of the transport of myelin proteins through the golgi apparatus. Cell Tissue Res 234:547-559.
    • (1983) Cell Tissue Res , vol.234 , pp. 547-559
    • Nussbaum, J.L.1    Roussel, G.2
  • 107
    • 0030937422 scopus 로고    scopus 로고
    • Syntaxin-4, VAMP-2, and/or VAMP-3/cellubrevin are fuctional target membrane and vesicle SNAP receptors for insulin stimulated GLUT-4 translocation in adipocytes
    • Olson AL, Knight JB, Pessin JE. 1997. Syntaxin-4, VAMP-2, and/or VAMP-3/cellubrevin are fuctional target membrane and vesicle SNAP receptors for insulin stimulated GLUT-4 translocation in adipocytes. Mol Cell Biol 17:2425-2435.
    • (1997) Mol Cell Biol , vol.17 , pp. 2425-2435
    • Olson, A.L.1    Knight, J.B.2    Pessin, J.E.3
  • 108
    • 0031030664 scopus 로고    scopus 로고
    • Caveolin-3 associates with developing T-tubules during muscle differentiation
    • Parton RG, Way M, Zorzi N, Stang E. 1997. Caveolin-3 associates with developing T-tubules during muscle differentiation. J Cell Biol 136:137-154.
    • (1997) J Cell Biol , vol.136 , pp. 137-154
    • Parton, R.G.1    Way, M.2    Zorzi, N.3    Stang, E.4
  • 109
    • 0024518799 scopus 로고
    • Inhibition of the synthesis of glycosphingolipids affects the translocation of proteolipid protein to the myelin membrane
    • Pasquini JM, Guarna MM, Besio-Moreno MA, Iturregui MT, Oteiza PI, Soto EF. 1989. Inhibition of the synthesis of glycosphingolipids affects the translocation of proteolipid protein to the myelin membrane. J Neurosci Res 22:289-296.
    • (1989) J Neurosci Res , vol.22 , pp. 289-296
    • Pasquini, J.M.1    Guarna, M.M.2    Besio-Moreno, M.A.3    Iturregui, M.T.4    Oteiza, P.I.5    Soto, E.F.6
  • 110
    • 0030946002 scopus 로고    scopus 로고
    • The active transport of myelin basic protein into the nucleus suggests a regulatory role in myelination
    • Pedraza L, Fidler L, Staugaitis SM, Coleman DR. 1997. The active transport of myelin basic protein into the nucleus suggests a regulatory role in myelination. Neuron 18:579-589.
    • (1997) Neuron , vol.18 , pp. 579-589
    • Pedraza, L.1    Fidler, L.2    Staugaitis, S.M.3    Coleman, D.R.4
  • 113
    • 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
  • 114
    • 0345683542 scopus 로고    scopus 로고
    • The MAL proteolipid is necessary for normal apical transport and accurate sorting of the influenza virus hemagglutinin in Madin-Darby Canine Kidney cells
    • Puertollano R, Martin-Belmonte F, Millan J, del Carmen de Marco M, Albar JP, Kremer L, Alonso MA. 1999. The MAL proteolipid is necessary for normal apical transport and accurate sorting of the influenza virus hemagglutinin in Madin-Darby Canine Kidney cells. J Cell Biol 145:141-151.
    • (1999) J Cell Biol , vol.145 , pp. 141-151
    • Puertollano, R.1    Martin-Belmonte, F.2    Millan, J.3    Del Carmen De Marco, M.4    Albar, J.P.5    Kremer, L.6    Alonso, M.A.7
  • 115
    • 0029929223 scopus 로고    scopus 로고
    • Identification of a novel syntaxin- And synaptobrevin/VAMP-binding protein, SNAP-23, expressed in non-neuronal tissues
    • Ravichandran V, Chawla A, Roche PA. 1996. Identification of a novel syntaxin- and synaptobrevin/VAMP-binding protein, SNAP-23, expressed in non-neuronal tissues. J Biol Chem 271:13300-13303.
    • (1996) J Biol Chem , vol.271 , pp. 13300-13303
    • Ravichandran, V.1    Chawla, A.2    Roche, P.A.3
  • 116
    • 0033962213 scopus 로고    scopus 로고
    • The oligodendroglia cytoskeleton in health and disease
    • Richter-Landsberg C. 2000. The oligodendroglia cytoskeleton in health and disease. J Neurosci Res 2000 59:11-18.
    • (2000) J Neurosci Res , vol.2000 , Issue.59 , pp. 11-18
    • Richter-Landsberg, C.1
  • 117
    • 0028143698 scopus 로고
    • Mechanisms of intracellular protein transport
    • Rothman JE. 1994. Mechanisms of intracellular protein transport. Nature 372:55-63.
    • (1994) Nature , vol.372 , pp. 55-63
    • Rothman, J.E.1
  • 119
  • 120
    • 0034651036 scopus 로고    scopus 로고
    • Multiple functions of the myelin-associated glycoprotein MAG (siglec-4a) in formation and maintenance of myelin
    • Schachner M, Bartsch U. 2000. Multiple functions of the myelin-associated glycoprotein MAG (siglec-4a) in formation and maintenance of myelin. Glia 29:154-165.
    • (2000) Glia , vol.29 , pp. 154-165
    • Schachner, M.1    Bartsch, U.2
  • 121
    • 0029111982 scopus 로고
    • Characterization of a rat gene rMAL, encoding a protein with four hydrophobic domains in central and peripheral myelin
    • Schaeren-Wiemers N, Valenzuela DM, Frank M, Schwab ME. 1995. Characterization of a rat gene rMAL, encoding a protein with four hydrophobic domains in central and peripheral myelin. J Neurosci 15:5753-5764.
    • (1995) J Neurosci , vol.15 , pp. 5753-5764
    • Schaeren-Wiemers, N.1    Valenzuela, D.M.2    Frank, M.3    Schwab, M.E.4
  • 122
    • 0032575477 scopus 로고    scopus 로고
    • Rab GTPases, directors of vesicle docking
    • Schimmöller F, Simon I, Pfeffer SR. 1998. Rab GTPases, directors of vesicle docking. J Biol Chem 273:22161-22164.
    • (1998) J Biol Chem , vol.273 , pp. 22161-22164
    • Schimmöller, F.1    Simon, I.2    Pfeffer, S.R.3
  • 123
    • 0022391252 scopus 로고
    • Electron microscopic immunocytochemical localization of myelin proteolipid protein and myelin basic protein in rat brain during myelination
    • Schwob VS, Clark HB, Agrawal D, Agrawal HG. 1985. Electron microscopic immunocytochemical localization of myelin proteolipid protein and myelin basic protein in rat brain during myelination. J Neurochem 45:559-571.
    • (1985) J Neurochem , vol.45 , pp. 559-571
    • Schwob, V.S.1    Clark, H.B.2    Agrawal, D.3    Agrawal, H.G.4
  • 124
    • 0027436941 scopus 로고
    • Rab proteins and the road maps for intracellular transport
    • Simons K, Zerial M. 1993. Rab proteins and the road maps for intracellular transport. Neuron 11:789-799.
    • (1993) Neuron , vol.11 , pp. 789-799
    • Simons, K.1    Zerial, M.2
  • 125
    • 0030949124 scopus 로고    scopus 로고
    • Functional rafts in cell membranes
    • Simons K, Ikonen E. 1997. Functional rafts in cell membranes. Nature 387:569-572.
    • (1997) Nature , vol.387 , pp. 569-572
    • Simons, K.1    Ikonen, E.2
  • 126
    • 0034597142 scopus 로고    scopus 로고
    • Assembly of myelin by association of proteolipid protein with cholesterol- and galactosylceramide-rich membrane domains
    • Simons M, Krämer EM, Thiele C, Stoffel W, Trotter J. 2000. Assembly of myelin by association of proteolipid protein with cholesterol- and galactosylceramide-rich membrane domains. J Cell Biol 151:1-13.
    • (2000) J Cell Biol , vol.151 , pp. 1-13
    • Simons, M.1    Krämer, E.M.2    Thiele, C.3    Stoffel, W.4    Trotter, J.5
  • 128
    • 0025297217 scopus 로고
    • Expression of myelin basic protein isoforms in nonglial cells
    • Staugaitis SM, Smith PR, Coleman DR. 1990. Expression of myelin basic protein isoforms in nonglial cells. J Cell Biol 110:1719-1727.
    • (1990) J Cell Biol , vol.110 , pp. 1719-1727
    • Staugaitis, S.M.1    Smith, P.R.2    Coleman, D.R.3
  • 130
    • 0029026392 scopus 로고
    • The synaptic vesicle cycle: A cascade of protein-protein interactions
    • Südhof TC. 1995. The synaptic vesicle cycle: a cascade of protein-protein interactions. Nature 375:645-653.
    • (1995) Nature , vol.375 , pp. 645-653
    • Südhof, T.C.1
  • 132
    • 0029890882 scopus 로고    scopus 로고
    • Expression of carbonic anhydrase II mRNA and protein in oligodendrocytes during toxic demyelination in the young adult mouse
    • Tansey FA, Zhang H, Cammer W. 1996. Expression of carbonic anhydrase II mRNA and protein in oligodendrocytes during toxic demyelination in the young adult mouse. Neurochem Res 21:411-416.
    • (1996) Neurochem Res , vol.21 , pp. 411-416
    • Tansey, F.A.1    Zhang, H.2    Cammer, W.3
  • 133
    • 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
  • 134
    • 0033559844 scopus 로고    scopus 로고
    • Transport of trembler-j mutant peripheral myelin protein 22 is blocked in the intermediate compartment and affects the transport of the wild-type protein by direct interaction
    • Tobler AR, Notterpek L, Naef R, Taylor V, Suter U, Shooter EM. 1999. Transport of trembler-j mutant peripheral myelin protein 22 is blocked in the intermediate compartment and affects the transport of the wild-type protein by direct interaction. J Neurosci 19:2027-2036.
    • (1999) J Neurosci , vol.19 , pp. 2027-2036
    • Tobler, A.R.1    Notterpek, L.2    Naef, R.3    Taylor, V.4    Suter, U.5    Shooter, E.M.6
  • 135
    • 0025651203 scopus 로고
    • Myelin-associated glycoprotein: Location and potential functions
    • Trapp BD. 1990. Myelin-associated glycoprotein: location and potential functions. Ann NY Acad Sci 605:29-43.
    • (1990) Ann NY Acad Sci , vol.605 , pp. 29-43
    • Trapp, B.D.1
  • 136
    • 0024447605 scopus 로고
    • The myelin-associated glycoprotein is enriched in multivesicular bodies and periaxonal membranes of actively myelinating oligodendrocytes
    • Trapp BD, Andrews SB, Cootauco C, Quartes RH. 1989. The myelin-associated glycoprotein is enriched in multivesicular bodies and periaxonal membranes of actively myelinating oligodendrocytes. J Cell Biol 109:2417-2426.
    • (1989) J Cell Biol , vol.109 , pp. 2417-2426
    • Trapp, B.D.1    Andrews, S.B.2    Cootauco, C.3    Quartes, R.H.4
  • 137
    • 0030939799 scopus 로고    scopus 로고
    • Differentiation and death of premyelinating oligodendrocytes in developing rodent brain
    • Trapp BD, Nishiyama A, Cheng D, Macklin W. 1997. Differentiation and death of premyelinating oligodendrocytes in developing rodent brain. J Cell Biol 137:459-468.
    • (1997) J Cell Biol , vol.137 , pp. 459-468
    • Trapp, B.D.1    Nishiyama, A.2    Cheng, D.3    Macklin, W.4
  • 138
    • 0033856546 scopus 로고    scopus 로고
    • GPI-anchored proteins and glycosphingolipid-rich rafts: Platforms for adhesion and signaling
    • Trotter J, Klein C, Krämer EM. 2000. GPI-anchored proteins and glycosphingolipid-rich rafts: platforms for adhesion and signaling. Neuroscientist 6:271-284.
    • (2000) Neuroscientist , vol.6 , pp. 271-284
    • Trotter, J.1    Klein, C.2    Krämer, E.M.3
  • 139
    • 0032006132 scopus 로고    scopus 로고
    • Transport of proteolipid protein to the plasma membrane does not depend on glycosphingolipid cotransport in oligodendrocyte cultures
    • van der Haar ME, Visser HW, de Vries H, Hoeckstra D. 1998. Transport of proteolipid protein to the plasma membrane does not depend on glycosphingolipid cotransport in oligodendrocyte cultures. J Neurosci Res 51:371-381.
    • (1998) J Neurosci Res , vol.51 , pp. 371-381
    • Van Der Haar, M.E.1    Visser, H.W.2    De Vries, H.3    Hoeckstra, D.4
  • 140
    • 0034047183 scopus 로고    scopus 로고
    • Intracellular transport, assembly, and degradation of wild-type and disease-linked mutant gap junction proteins
    • VanSlyke JK, Deschenes SM, Musil LS. 2000. Intracellular transport, assembly, and degradation of wild-type and disease-linked mutant gap junction proteins. Mol Biol Cell 11:1933-1946.
    • (2000) Mol Biol Cell , vol.11 , pp. 1933-1946
    • VanSlyke, J.K.1    Deschenes, S.M.2    Musil, L.S.3
  • 141
    • 0033179888 scopus 로고    scopus 로고
    • Membrane tethering in intracellular transport
    • Waters MG, Pfefier SR. 1999. Membrane tethering in intracellular transport. Curr Opin Cell Biol 11:453-459.
    • (1999) Curr Opin Cell Biol , vol.11 , pp. 453-459
    • Waters, M.G.1    Pfefier, S.R.2
  • 142
    • 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
  • 144
    • 0027487979 scopus 로고
    • A myelin proteolipid protein-LacZ fusion protein is developmentally regulated and targeted to the myelin membrane in transgenic mice
    • Whight PA, Duchala CS, Readhead C, Macklin WB. 1993. A myelin proteolipid protein-LacZ fusion protein is developmentally regulated and targeted to the myelin membrane in transgenic mice. J Cell Biol 123:443-454.
    • (1993) J Cell Biol , vol.123 , pp. 443-454
    • Whight, P.A.1    Duchala, C.S.2    Readhead, C.3    Macklin, W.B.4
  • 145
    • 0032510397 scopus 로고    scopus 로고
    • Vesicle transport: More work for the Rabs?
    • Woodman P. 1998. Vesicle transport: More work for the Rabs? Curr Biol 8:R199-R201.
    • (1998) Curr Biol , vol.8
    • Woodman, P.1
  • 148
    • 0034639930 scopus 로고    scopus 로고
    • The proteolipid protein gene and myelin disorders in man and animal models
    • Yool DA, Edgar JM, Montague P, Malcolm S. 2000. The proteolipid protein gene and myelin disorders in man and animal models. Hum Mol Genet 9:987-992.
    • (2000) Hum Mol Genet , vol.9 , pp. 987-992
    • Yool, D.A.1    Edgar, J.M.2    Montague, P.3    Malcolm, S.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.