메뉴 건너뛰기




Volumn 9, Issue 7, 2014, Pages

The lateral membrane organization and dynamics of myelin proteins PLP and MBP are dictated by distinct galactolipids and the extracellular matrix

Author keywords

[No Author keywords available]

Indexed keywords

FIBRONECTIN; GALACTOLIPID; GALACTOSYLCERAMIDE; MEROSIN; MYELIN BASIC PROTEIN; PROTEOLIPID PROTEIN; SULFATIDE; LAMININ; MBP PROTEIN, RAT; PLP1 PROTEIN, RAT;

EID: 84903889611     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0101834     Document Type: Article
Times cited : (33)

References (61)
  • 1
    • 0035066639 scopus 로고    scopus 로고
    • Biology of oligodendrocyte and myelin in the mammalian central nervous system
    • Baumann N, Pham-Dinh D (2001) Biology of oligodendrocyte and myelin in the mammalian central nervous system. Physiol Rev 81: 871-927.
    • (2001) Physiol Rev , vol.81 , pp. 871-927
    • Baumann, N.1    Pham-Dinh, D.2
  • 2
    • 80053109845 scopus 로고    scopus 로고
    • Central nervous system myelin: Structure, synthesis and assembly
    • doi:10.1016/j.tcb.2011.06.004
    • Aggarwal S, Yurlova L, Simons M (2011) Central nervous system myelin: structure, synthesis and assembly. Trends Cell Biol 21: 585-593. doi:10.1016/j.tcb.2011.06.004.
    • (2011) Trends Cell Biol , vol.21 , pp. 585-593
    • Aggarwal, S.1    Yurlova, L.2    Simons, M.3
  • 3
    • 77951929406 scopus 로고    scopus 로고
    • On the biogenesis of myelin membranes: Sorting, trafficking and cell polarity
    • doi:10.1016/j.febslet.2009.10.085
    • Baron W, Hoekstra D (2010) On the biogenesis of myelin membranes: sorting, trafficking and cell polarity. FEBS Lett 584: 1760-1770. doi:10.1016/j.febslet.2009.10.085.
    • (2010) FEBS Lett , vol.584 , pp. 1760-1770
    • Baron, W.1    Hoekstra, D.2
  • 4
    • 70349932435 scopus 로고    scopus 로고
    • Oligodendrocyte development and myelin biogenesis: Parsing out the roles of glycosphingolipids
    • doi:10.1152/physiol.00016.2009
    • Jackman N, Ishii A, Bansal R (2009) Oligodendrocyte development and myelin biogenesis: parsing out the roles of glycosphingolipids. Physiology (Bethesda) 24: 290-297. doi:10.1152/physiol.00016.2009.
    • (2009) Physiology (Bethesda) , vol.24 , pp. 290-297
    • Jackman, N.1    Ishii, A.2    Bansal, R.3
  • 5
    • 77949486537 scopus 로고    scopus 로고
    • Myelin, DIGs, and membrane rafts in the central nervous system
    • doi:10.1016/j.prostaglandins.2009.04.005
    • Dupree JL, Pomicter AD (2010) Myelin, DIGs, and membrane rafts in the central nervous system. Prostaglandins Other Lipid Mediat 91: 118-129. doi:10.1016/j.prostaglandins.2009.04.005.
    • (2010) Prostaglandins Other Lipid Mediat , vol.91 , pp. 118-129
    • Dupree, J.L.1    Pomicter, A.D.2
  • 6
    • 0027273759 scopus 로고
    • Vesicular transport of myelin proteolipid and cerebroside sulfates to the myelin membrane
    • doi:10.1002/jnr.490350407
    • Brown MC, Moreno MB, Bongarzone ER, Cohen PD, Soto EF, et al. (1993) Vesicular transport of myelin proteolipid and cerebroside sulfates to the myelin membrane. J Neurosci Res 35: 402-408. doi:10.1002/jnr.490350407.
    • (1993) J Neurosci Res , vol.35 , pp. 402-408
    • Brown, M.C.1    Moreno, M.B.2    Bongarzone, E.R.3    Cohen, P.D.4    Soto, E.F.5
  • 7
    • 33748487414 scopus 로고    scopus 로고
    • Myelin basic protein: A multifunctional protein
    • doi:10.1007/s00018-006-6094-7
    • Boggs JM (2006) Myelin basic protein: a multifunctional protein. Cell Mol Life Sci 63: 1945-1961. doi:10.1007/s00018-006-6094-7.
    • (2006) Cell Mol Life Sci , vol.63 , pp. 1945-1961
    • Boggs, J.M.1
  • 8
    • 77951925532 scopus 로고    scopus 로고
    • Participation of galactosylceramide and sulfatide in glycosynapses between oligodendrocyte or myelin membranes
    • doi:10.1016/j.febslet.2009.11.074
    • Boggs JM, Gao W, Zhao J, Park H-J, Liu Y, et al. (2010) Participation of galactosylceramide and sulfatide in glycosynapses between oligodendrocyte or myelin membranes. FEBS Lett 584: 1771-1778. doi:10.1016/j.febslet.2009.11.074.
    • (2010) FEBS Lett , vol.584 , pp. 1771-1778
    • Boggs, J.M.1    Gao, W.2    Zhao, J.3    Park, H.-J.4    Liu, Y.5
  • 9
    • 43149116803 scopus 로고    scopus 로고
    • Signal transduction pathways involved in interaction of galactosylceramide/sulfatide-containing liposomes with cultured oligodendrocytes and requirement for myelin basic protein and glycosphingolipids
    • doi:10.1002/jnr.21603
    • Boggs JM, Gao W, Hirahara Y (2008) Signal transduction pathways involved in interaction of galactosylceramide/sulfatide-containing liposomes with cultured oligodendrocytes and requirement for myelin basic protein and glycosphingolipids. J Neurosci Res 86: 1448-1458. doi:10.1002/jnr.21603.
    • (2008) J Neurosci Res , vol.86 , pp. 1448-1458
    • Boggs, J.M.1    Gao, W.2    Hirahara, Y.3
  • 10
    • 40849086666 scopus 로고    scopus 로고
    • Myelin glycosphingolipids, galactosylceramide and sulfatide, participate in carbohydrate-carbohydrate interactions between apposed membranes and may form glycosynapses between oligodendrocyte and/or myelin membranes
    • doi:10.1016/j.bbagen.2007.10.015
    • Boggs JM, Gao W, Hirahara Y (2008) Myelin glycosphingolipids, galactosylceramide and sulfatide, participate in carbohydrate-carbohydrate interactions between apposed membranes and may form glycosynapses between oligodendrocyte and/or myelin membranes. Biochim Biophys Acta 1780: 445-455. doi:10.1016/j.bbagen.2007.10.015.
    • (2008) Biochim Biophys Acta , vol.1780 , pp. 445-455
    • Boggs, J.M.1    Gao, W.2    Hirahara, Y.3
  • 11
    • 0024456055 scopus 로고
    • Organization of oligodendroglial membrane sheets: II. Galactocerebroside:Antibody interactions signal changes in cytoskeleton and myelin basic protein
    • doi:10.1002/jnr.490240212
    • Dyer CA, Benjamins JA (1989) Organization of oligodendroglial membrane sheets: II. Galactocerebroside:antibody interactions signal changes in cytoskeleton and myelin basic protein. J Neurosci Res 24: 212-221. doi:10.1002/jnr.490240212.
    • (1989) J Neurosci Res , vol.24 , pp. 212-221
    • Dyer, C.A.1    Benjamins, J.A.2
  • 12
    • 0026350796 scopus 로고
    • Galactocerebroside and sulfatide independently mediate Ca2+ responses in oligodendrocytes
    • doi:10.1002/jnr.490300414
    • Dyer CA, Benjamins JA (1991) Galactocerebroside and sulfatide independently mediate Ca2+ responses in oligodendrocytes. J Neurosci Res 30: 699-711. doi:10.1002/jnr.490300414.
    • (1991) J Neurosci Res , vol.30 , pp. 699-711
    • Dyer, C.A.1    Benjamins, J.A.2
  • 13
    • 33750436896 scopus 로고    scopus 로고
    • Myelin basic protein-dependent plasma membrane reorganization in the formation of myelin
    • doi:10.1038/sj.emboj.7601376
    • Fitzner D, Schneider A, Kippert A, Möbius W, Willig KI, et al. (2006) Myelin basic protein-dependent plasma membrane reorganization in the formation of myelin. EMBO J 25: 5037-5048. doi:10.1038/sj.emboj.7601376.
    • (2006) EMBO J , vol.25 , pp. 5037-5048
    • Fitzner, D.1    Schneider, A.2    Kippert, A.3    Möbius, W.4    Willig, K.I.5
  • 14
    • 80053930455 scopus 로고    scopus 로고
    • Glia unglued: How signals from the extracellular matrix regulate the development of myelinating glia
    • doi:10.1002/dneu.20966
    • Colognato H, Tzvetanova ID (2011) Glia unglued: how signals from the extracellular matrix regulate the development of myelinating glia. Dev Neurobiol 71: 924-955. doi:10.1002/dneu.20966.
    • (2011) Dev Neurobiol , vol.71 , pp. 924-955
    • Colognato, H.1    Tzvetanova, I.D.2
  • 16
    • 0242266910 scopus 로고    scopus 로고
    • Integrin-linked kinase is required for laminin-2-induced oligodendrocyte cell spreading and CNS myelination
    • doi:10.1083/jcb.200304154
    • Chun SJ, Rasband MN, Sidman RL, Habib AA, Vartanian T (2003) Integrin-linked kinase is required for laminin-2-induced oligodendrocyte cell spreading and CNS myelination. J Cell Biol 163: 397-408. doi:10.1083/jcb. 200304154.
    • (2003) J Cell Biol , vol.163 , pp. 397-408
    • Chun, S.J.1    Rasband, M.N.2    Sidman, R.L.3    Habib, A.A.4    Vartanian, T.5
  • 17
    • 0036850183 scopus 로고    scopus 로고
    • CNS integrins switch growth factor signalling to promote target-dependent survival
    • doi:10.1038/ncb865
    • Colognato H, Baron W, Avellana-Adalid V, Relvas JB, Baron-Van Evercooren A, et al. (2002) CNS integrins switch growth factor signalling to promote target-dependent survival. Nat Cell Biol 4: 833-841. doi:10.1038/ncb865.
    • (2002) Nat Cell Biol , vol.4 , pp. 833-841
    • Colognato, H.1    Baron, W.2    Avellana-Adalid, V.3    Relvas, J.B.4    Baron-Van Evercooren, A.5
  • 18
    • 0032861273 scopus 로고    scopus 로고
    • Laminin-2/integrin interactions enhance myelin membrane formation by oligodendrocytes
    • doi:10.1006/mcne.1999.0781
    • Buttery PC, ffrench-Constant C (1999) Laminin-2/integrin interactions enhance myelin membrane formation by oligodendrocytes. Mol Cell Neurosci 14: 199-212. doi:10.1006/mcne.1999.0781.
    • (1999) Mol Cell Neurosci , vol.14 , pp. 199-212
    • Buttery, P.C.1    Ffrench-Constant, C.2
  • 19
    • 0035838420 scopus 로고    scopus 로고
    • Expression of dominant-negative and chimeric subunits reveals an essential role for beta1 integrin during myelination
    • Relvas JB, Setzu A, Baron W, Buttery PC, LaFlamme SE, et al. (2001) Expression of dominant-negative and chimeric subunits reveals an essential role for beta1 integrin during myelination. Curr Biol 11: 1039-1043.
    • (2001) Curr Biol , vol.11 , pp. 1039-1043
    • Relvas, J.B.1    Setzu, A.2    Baron, W.3    Buttery, P.C.4    LaFlamme, S.E.5
  • 20
    • 33748797722 scopus 로고    scopus 로고
    • Fibronectin impedes "myelin" sheet-directed flow in oligodendrocytes: A role for a beta 1 integrin-mediated PKC signaling pathway in vesicular trafficking
    • doi:10.1016/j.mcn.2006.07.001
    • Sisková Z, Baron W, de Vries H, Hoekstra D (2006) Fibronectin impedes "myelin" sheet-directed flow in oligodendrocytes: a role for a beta 1 integrin-mediated PKC signaling pathway in vesicular trafficking. Mol Cell Neurosci 33: 150-159. doi:10.1016/j.mcn.2006.07.001.
    • (2006) Mol Cell Neurosci , vol.33 , pp. 150-159
    • Sisková, Z.1    Baron, W.2    De Vries, H.3    Hoekstra, D.4
  • 21
    • 84887083278 scopus 로고    scopus 로고
    • Fibronectin in tissue regeneration: Timely disassembly of the scaffold is necessary to complete the build
    • doi:10.1007/s00018-013-1350-0
    • Stoffels JMJ, Zhao C, Baron W (2013) Fibronectin in tissue regeneration: timely disassembly of the scaffold is necessary to complete the build. Cell Mol Life Sci 70: 4243-4253. doi:10.1007/s00018-013-1350-0.
    • (2013) Cell Mol Life Sci , vol.70 , pp. 4243-4253
    • Stoffels, J.M.J.1    Zhao, C.2    Baron, W.3
  • 22
    • 35448936315 scopus 로고    scopus 로고
    • The extracellular matrix in multiple sclerosis pathology
    • doi:10.1111/j.1471-4159.2007.04897.x
    • Van Horssen J, Dijkstra CD, de Vries HE (2007) The extracellular matrix in multiple sclerosis pathology. J Neurochem 103: 1293-1301. doi:10.1111/j.1471-4159.2007.04897.x.
    • (2007) J Neurochem , vol.103 , pp. 1293-1301
    • Van Horssen, J.1    Dijkstra, C.D.2    De Vries, H.E.3
  • 23
    • 0034304851 scopus 로고    scopus 로고
    • Lipid rafts and signal transduction
    • doi:10.1038/35036052
    • Simons K, Toomre D (2000) Lipid rafts and signal transduction. Nat Rev Mol Cell Biol 1: 31-39. doi:10.1038/35036052.
    • (2000) Nat Rev Mol Cell Biol , vol.1 , pp. 31-39
    • Simons, K.1    Toomre, D.2
  • 24
    • 0030949124 scopus 로고    scopus 로고
    • Functional rafts in cell membranes
    • doi:10.1038/42408
    • Simons K, Ikonen E (1997) Functional rafts in cell membranes. Nature 387: 569-572. doi:10.1038/42408.
    • (1997) Nature , vol.387 , pp. 569-572
    • Simons, K.1    Ikonen, E.2
  • 25
    • 0017192686 scopus 로고
    • Mobility measurement by analysis of fluorescence photobleaching recovery kinetics
    • doi:10.1016/S0006-3495(76)85755-4
    • Axelrod D, Koppel DE, Schlessinger J, Elson E, Webb WW (1976) Mobility measurement by analysis of fluorescence photobleaching recovery kinetics. Biophys J 16: 1055-1069. doi:10.1016/S0006-3495(76)85755-4.
    • (1976) Biophys J , vol.16 , pp. 1055-1069
    • Axelrod, D.1    Koppel, D.E.2    Schlessinger, J.3    Elson, E.4    Webb, W.W.5
  • 26
    • 0022545162 scopus 로고
    • Scanning fluorescence correlation spectroscopy. I. Theory and simulation of aggregation measurements
    • Petersen NO (1986) Scanning fluorescence correlation spectroscopy. I. Theory and simulation of aggregation measurements. Biophys J 49: 809-815.
    • (1986) Biophys J , vol.49 , pp. 809-815
    • Petersen, N.O.1
  • 27
    • 82955214736 scopus 로고    scopus 로고
    • Circular scanning fluorescence correlation spectroscopy on membranes
    • Petrášek Z, Derenko S, Schwille P (2011) Circular scanning fluorescence correlation spectroscopy on membranes. Opt Express 19: 25006-25021.
    • (2011) Opt Express , vol.19 , pp. 25006-25021
    • Petrášek, Z.1    Derenko, S.2    Schwille, P.3
  • 28
    • 4143135216 scopus 로고    scopus 로고
    • Spatial-temporal studies of membrane dynamics: Scanning fluorescence correlation spectroscopy (SFCS)
    • doi:10.1529/biophysj.103.036483
    • Ruan Q, Cheng MA, Levi M, Gratton E, Mantulin WW (2004) Spatial-temporal studies of membrane dynamics: scanning fluorescence correlation spectroscopy (SFCS). Biophys J 87: 1260-1267. doi:10.1529/biophysj.103.036483.
    • (2004) Biophys J , vol.87 , pp. 1260-1267
    • Ruan, Q.1    Cheng, M.A.2    Levi, M.3    Gratton, E.4    Mantulin, W.W.5
  • 29
    • 17844394185 scopus 로고    scopus 로고
    • Fluctuation Correlation Spectroscopy with a Laser-Scanning Microscope: Exploiting the Hidden Time Structure
    • doi:10.1529/biophysj.105.061788
    • Digman MA, Sengupta P, Wiseman PW, Brown CM, Horwitz AR, et al. (2005) Fluctuation Correlation Spectroscopy with a Laser-Scanning Microscope: Exploiting the Hidden Time Structure. Biophys J 88: L33-L36. doi:10.1529/biophysj.105.061788.
    • (2005) Biophys J , vol.88
    • Digman, M.A.1    Sengupta, P.2    Wiseman, P.W.3    Brown, C.M.4    Horwitz, A.R.5
  • 30
    • 23244441649 scopus 로고    scopus 로고
    • Measuring Fast Dynamics in Solutions and Cells with a Laser Scanning Microscope
    • doi:10.1529/biophysj.105.062836
    • Digman MA, Brown CM, Sengupta P, Wiseman PW, Horwitz AR, et al. (2005) Measuring Fast Dynamics in Solutions and Cells with a Laser Scanning Microscope. Biophys J 89: 1317-1327. doi:10.1529/biophysj.105.062836.
    • (2005) Biophys J , vol.89 , pp. 1317-1327
    • Digman, M.A.1    Brown, C.M.2    Sengupta, P.3    Wiseman, P.W.4    Horwitz, A.R.5
  • 31
    • 84882950477 scopus 로고    scopus 로고
    • Pulsed interleaved excitation fluctuation imaging
    • doi:10.1016/j.bpj.2013.05.059
    • Hendrix J, Schrimpf W, Höller M, Lamb DC (2013) Pulsed interleaved excitation fluctuation imaging. Biophys J 105: 848-861. doi:10.1016/j.bpj.2013. 05.059.
    • (2013) Biophys J , vol.105 , pp. 848-861
    • Hendrix, J.1    Schrimpf, W.2    Höller, M.3    Lamb, D.C.4
  • 32
    • 0030017964 scopus 로고    scopus 로고
    • OLN-93: A new permanent oligodendroglia cell line derived from primary rat brain glial cultures
    • doi:10.1002/(SICI)1097-4547(19960715)45:2〈16
    • Richter-Landsberg C, Heinrich M (1996) OLN-93: a new permanent oligodendroglia cell line derived from primary rat brain glial cultures. J Neurosci Res 45: 161-173. doi:10.1002/(SICI)1097-4547(19960715)45:2〈161:: AID-JNR8〉3.0.CO;2-8.
    • (1996) J Neurosci Res , vol.45 , pp. 161-173
    • Richter-Landsberg, C.1    Heinrich, M.2
  • 33
    • 84891686978 scopus 로고    scopus 로고
    • Regulation of cell proliferation by nucleocytoplasmic dynamics of postnatal and embryonic exon-II-containing MBP isoforms
    • doi:10.1016/j.bbamcr.2013.11.026
    • Ozgen H, Kahya N, de Jonge JC, Smith GST, Harauz G, et al. (2013) Regulation of cell proliferation by nucleocytoplasmic dynamics of postnatal and embryonic exon-II-containing MBP isoforms. Biochim Biophys Acta 1843: 517-530. doi:10.1016/j.bbamcr.2013.11.026.
    • (2013) Biochim Biophys Acta , vol.1843 , pp. 517-530
    • Ozgen, H.1    Kahya, N.2    De Jonge, J.C.3    Smith, G.S.T.4    Harauz, G.5
  • 34
    • 79751472668 scopus 로고    scopus 로고
    • Classical 18.5-and 21.5-kDa isoforms of myelin basic protein inhibit calcium influx into oligodendroglial cells, in contrast to golli isoforms
    • doi:10.1002/jnr.22570
    • Smith GST, Paez PM, Spreuer V, Campagnoni CW, Boggs JM, et al. (2011) Classical 18.5-and 21.5-kDa isoforms of myelin basic protein inhibit calcium influx into oligodendroglial cells, in contrast to golli isoforms. J Neurosci Res 89: 467-480. doi:10.1002/jnr.22570.
    • (2011) J Neurosci Res , vol.89 , pp. 467-480
    • Smith, G.S.T.1    Paez, P.M.2    Spreuer, V.3    Campagnoni, C.W.4    Boggs, J.M.5
  • 35
    • 29144463712 scopus 로고    scopus 로고
    • The function of neurofascin155 in oligodendrocytes is regulated by metalloprotease-mediated cleavage and ectodomain shedding
    • doi:10.1016/j.yexcr.2005.11.014
    • Maier O, van der Heide T, Johnson R, de Vries H, Baron W, et al. (2006) The function of neurofascin155 in oligodendrocytes is regulated by metalloprotease-mediated cleavage and ectodomain shedding. Exp Cell Res 312: 500-511. doi:10.1016/j.yexcr.2005.11.014.
    • (2006) Exp Cell Res , vol.312 , pp. 500-511
    • Maier, O.1    Van Der Heide, T.2    Johnson, R.3    De Vries, H.4    Baron, W.5
  • 36
    • 0034597142 scopus 로고    scopus 로고
    • Assembly of myelin by association of proteolipid protein with cholesterol- and galactosylcer-amide-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 galactosylcer-amide-rich membrane domains. J Cell Biol 151: 143-154.
    • (2000) J Cell Biol , vol.151 , pp. 143-154
    • Simons, M.1    Krämer, E.M.2    Thiele, C.3    Stoffel, W.4    Trotter, J.5
  • 37
    • 13444274593 scopus 로고    scopus 로고
    • Alteration of the extracellular matrix interferes with raft association of neurofascin in oligodendrocytes. Potential significance for multiple sclerosis?
    • doi:10.1016/j.mcn.2004.09.012
    • Maier O, van der Heide T, van Dam A-M, Baron W, de Vries H, et al. (2005) Alteration of the extracellular matrix interferes with raft association of neurofascin in oligodendrocytes. Potential significance for multiple sclerosis? Mol Cell Neurosci 28: 390-401. doi:10.1016/j.mcn.2004.09.012.
    • (2005) Mol Cell Neurosci , vol.28 , pp. 390-401
    • Maier, O.1    Van Der Heide, T.2    Van Dam, A.-M.3    Baron, W.4    De Vries, H.5
  • 38
    • 41149128817 scopus 로고    scopus 로고
    • Sorting signals and regulation of cognate basolateral trafficking in myelin biogenesis
    • doi:10.1002/jnr.21556
    • Klunder B, Baron W, Schrage C, de Jonge J, de Vries H, et al. (2008) Sorting signals and regulation of cognate basolateral trafficking in myelin biogenesis. J Neurosci Res 86: 1007-1016. doi:10.1002/jnr.21556.
    • (2008) J Neurosci Res , vol.86 , pp. 1007-1016
    • Klunder, B.1    Baron, W.2    Schrage, C.3    De Jonge, J.4    De Vries, H.5
  • 39
    • 0019891130 scopus 로고
    • Monoclonal antibodies (O1 to O4) to oligodendrocyte cell surfaces: An immunocytological study in the central nervous system
    • Sommer I, Schachner M (1981) Monoclonal antibodies (O1 to O4) to oligodendrocyte cell surfaces: an immunocytological study in the central nervous system. Dev Biol 83: 311-327.
    • (1981) Dev Biol , vol.83 , pp. 311-327
    • Sommer, I.1    Schachner, M.2
  • 40
    • 33845764296 scopus 로고    scopus 로고
    • A guided tour into subcellular colocalization analysis in light microscopy
    • doi:10.1111/j.1365-2818.2006.01706.x
    • Bolte S, Cordelières FP (2006) A guided tour into subcellular colocalization analysis in light microscopy. J Microsc 224: 213-232. doi:10.1111/j.1365-2818.2006.01706.x.
    • (2006) J Microsc , vol.224 , pp. 213-232
    • Bolte, S.1    Cordelières, F.P.2
  • 41
    • 84934437530 scopus 로고    scopus 로고
    • Implementation and Application of Pulsed Interleaved Excitation for Dual-Color FCS and RICS
    • doi:10.1007/978-1-62703-649-8-30
    • Hendrix J, Lamb DC (2014) Implementation and Application of Pulsed Interleaved Excitation for Dual-Color FCS and RICS. Methods Mol Biol 1076: 653-682. doi:10.1007/978-1-62703-649-8-30.
    • (2014) Methods Mol Biol , vol.1076 , pp. 653-682
    • Hendrix, J.1    Lamb, D.C.2
  • 42
    • 79952347049 scopus 로고    scopus 로고
    • The transcriptional co-activator LEDGF/p75 displays a dynamic scan-and-lock mechanism for chromatin tethering
    • doi:10.1093/nar/gkq933
    • Hendrix J, Gijsbers R, De Rijck J, Voet A, Hotta J, et al. (2011) The transcriptional co-activator LEDGF/p75 displays a dynamic scan-and-lock mechanism for chromatin tethering. Nucleic Acids Res 39: 1310-1325. doi:10.1093/nar/gkq933.
    • (2011) Nucleic Acids Res , vol.39 , pp. 1310-1325
    • Hendrix, J.1    Gijsbers, R.2    De Rijck, J.3    Voet, A.4    Hotta, J.5
  • 43
    • 45949105768 scopus 로고    scopus 로고
    • Polarity development in oligodendrocytes: Sorting and trafficking of myelin components
    • doi:10.1007/s12031-007-9024-8
    • Maier O, Hoekstra D, Baron W (2008) Polarity development in oligodendrocytes: sorting and trafficking of myelin components. J Mol Neurosci 35: 35-53. doi:10.1007/s12031-007-9024-8.
    • (2008) J Mol Neurosci , vol.35 , pp. 35-53
    • Maier, O.1    Hoekstra, D.2    Baron, W.3
  • 44
    • 0034611005 scopus 로고    scopus 로고
    • Sphingolipid-cholesterol rafts diffuse as small entities in the plasma membrane of mammalian cells
    • doi:10.1083/jcb.148.5.997
    • Pralle A, Keller P, Florin E-L, Simons K, Hörber JKH (2000) Sphingolipid-cholesterol rafts diffuse as small entities in the plasma membrane of mammalian cells. J Cell Biol 148: 997-1008. doi:10.1083/jcb.148.5.997.
    • (2000) J Cell Biol , vol.148 , pp. 997-1008
    • Pralle, A.1    Keller, P.2    Florin, E.-L.3    Simons, K.4    Hörber, J.K.H.5
  • 45
    • 18744371895 scopus 로고    scopus 로고
    • Developmental partitioning of myelin basic protein into membrane microdomains
    • doi:10.1002/jnr.20452
    • DeBruin LS, Haines JD, Wellhauser LA, Radeva G, Schonmann V, et al. (2005) Developmental partitioning of myelin basic protein into membrane microdomains. J Neurosci Res 80: 211-225. doi:10.1002/jnr.20452.
    • (2005) J Neurosci Res , vol.80 , pp. 211-225
    • DeBruin, L.S.1    Haines, J.D.2    Wellhauser, L.A.3    Radeva, G.4    Schonmann, V.5
  • 46
    • 84866414194 scopus 로고    scopus 로고
    • Quantifying lipid diffusion by fluorescence correlation spectroscopy: A critical treatise
    • doi:10.1021/la302596h
    • Heinemann F, Betaneli V, Thomas FA, Schwille P (2012) Quantifying lipid diffusion by fluorescence correlation spectroscopy: a critical treatise. Langmuir 28: 13395-13404. doi:10.1021/la302596h.
    • (2012) Langmuir , vol.28 , pp. 13395-13404
    • Heinemann, F.1    Betaneli, V.2    Thomas, F.A.3    Schwille, P.4
  • 47
    • 34547124343 scopus 로고    scopus 로고
    • Signaling through a G Protein-coupled receptor and its corresponding G protein follows a stoichiometrically limited model
    • doi:10.1074/jbc.M701558200
    • Philip F, Sengupta P, Scarlata S (2007) Signaling through a G Protein-coupled receptor and its corresponding G protein follows a stoichiometrically limited model. J Biol Chem 282: 19203-19216. doi:10.1074/jbc.M701558200.
    • (2007) J Biol Chem , vol.282 , pp. 19203-19216
    • Philip, F.1    Sengupta, P.2    Scarlata, S.3
  • 48
    • 84873345336 scopus 로고    scopus 로고
    • Fibronectin aggregation in multiple sclerosis lesions impairs remyelination
    • doi:10.1093/brain/aws313
    • Stoffels JMJ, de Jonge JC, Stancic M, Nomden A, van Strien ME, et al. (2013) Fibronectin aggregation in multiple sclerosis lesions impairs remyelination. Brain 136: 116-131. doi:10.1093/brain/aws313.
    • (2013) Brain , vol.136 , pp. 116-131
    • Stoffels, J.M.J.1    De Jonge, J.C.2    Stancic, M.3    Nomden, A.4    Van Strien, M.E.5
  • 49
    • 0037007067 scopus 로고    scopus 로고
    • Paranodal junction formation and spermatogenesis require sulfoglycolipids
    • doi:10.1073/pnas.032068299
    • Honke K, Hirahara Y, Dupree J, Suzuki K, Popko B, et al. (2002) Paranodal junction formation and spermatogenesis require sulfoglycolipids. Proc Natl Acad Sci USA 99: 4227-4232. doi:10.1073/pnas.032068299.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 4227-4232
    • Honke, K.1    Hirahara, Y.2    Dupree, J.3    Suzuki, K.4    Popko, B.5
  • 50
    • 0031983184 scopus 로고    scopus 로고
    • Composition and biophysical properties of myelin lipid define the neurological defects in galactocerebrosideand sulfatide-deficient mice
    • Bosio A, Binczek E, Haupt WF, Stoffel W (1998) Composition and biophysical properties of myelin lipid define the neurological defects in galactocerebrosideand sulfatide-deficient mice. J Neurochem 70: 308-315.
    • (1998) J Neurochem , vol.70 , pp. 308-315
    • Bosio, A.1    Binczek, E.2    Haupt, W.F.3    Stoffel, W.4
  • 51
    • 73949099691 scopus 로고    scopus 로고
    • Myelin protein composition is altered in mice lacking either sulfated or both sulfated and non-sulfated galactolipids
    • doi:10.1111/j.1471-4159.2009.06464.x
    • Fewou SN, Fernandes A, Stockdale K, Francone VP, Dupree JL, et al. (2010) Myelin protein composition is altered in mice lacking either sulfated or both sulfated and non-sulfated galactolipids. J Neurochem 112: 599-610. doi:10.1111/j.1471-4159.2009.06464.x.
    • (2010) J Neurochem , vol.112 , pp. 599-610
    • Fewou, S.N.1    Fernandes, A.2    Stockdale, K.3    Francone, V.P.4    Dupree, J.L.5
  • 52
    • 2342446570 scopus 로고    scopus 로고
    • Co-clustering of galactosylceramide and membrane proteins in oligodendrocyte membranes on interaction with polyvalent carbohydrate and prevention by an intact cytoskeleton
    • doi:10.1002/jnr.20080
    • Boggs JM, Wang H (2004) Co-clustering of galactosylceramide and membrane proteins in oligodendrocyte membranes on interaction with polyvalent carbohydrate and prevention by an intact cytoskeleton. J Neurosci Res 76: 342-355. doi:10.1002/jnr.20080.
    • (2004) J Neurosci Res , vol.76 , pp. 342-355
    • Boggs, J.M.1    Wang, H.2
  • 53
    • 0028129521 scopus 로고
    • Myelin basic protein mediates extracellular signals that regulate microtubule stability in oligodendrocyte membrane sheets
    • doi:10.1002/jnr.490390112
    • Dyer CA, Philibotte TM, Wolf MK, Billings-Gagliardi S (1994) Myelin basic protein mediates extracellular signals that regulate microtubule stability in oligodendrocyte membrane sheets. J Neurosci Res 39: 97-107. doi:10.1002/jnr. 490390112.
    • (1994) J Neurosci Res , vol.39 , pp. 97-107
    • Dyer, C.A.1    Philibotte, T.M.2    Wolf, M.K.3    Billings-Gagliardi, S.4
  • 54
    • 2942655668 scopus 로고    scopus 로고
    • Dynamics of putative raft-associated proteins at the cell surface
    • doi:10.1083/jcb.200312170
    • Kenworthy AK, Nichols BJ, Remmert CL, Hendrix GM, Kumar M, et al. (2004) Dynamics of putative raft-associated proteins at the cell surface. J Cell Biol 165: 735-746. doi:10.1083/jcb.200312170.
    • (2004) J Cell Biol , vol.165 , pp. 735-746
    • Kenworthy, A.K.1    Nichols, B.J.2    Remmert, C.L.3    Hendrix, G.M.4    Kumar, M.5
  • 55
    • 33645294105 scopus 로고    scopus 로고
    • Fluorescence correlation studies of lipid domains in model membranes
    • doi:10.1080/09687860500489099
    • Kahya N, Schwille P (2006) Fluorescence correlation studies of lipid domains in model membranes. Mol Membr Biol 23: 29-39. doi:10.1080/ 09687860500489099.
    • (2006) Mol Membr Biol , vol.23 , pp. 29-39
    • Kahya, N.1    Schwille, P.2
  • 56
    • 84861079568 scopus 로고    scopus 로고
    • Elucidating membrane structure and protein behavior using giant plasma membrane vesicles
    • doi:10.1038/nprot.2012.059
    • Sezgin E, Kaiser H-J, Baumgart T, Schwille P, Simons K, et al. (2012) Elucidating membrane structure and protein behavior using giant plasma membrane vesicles. Nat Protoc 7: 1042-1051. doi:10.1038/nprot.2012.059.
    • (2012) Nat Protoc , vol.7 , pp. 1042-1051
    • Sezgin, E.1    Kaiser, H.-J.2    Baumgart, T.3    Schwille, P.4    Simons, K.5
  • 57
    • 0037458140 scopus 로고    scopus 로고
    • Regulation of integrin growth factor interactions in oligodendrocytes by lipid raft microdomains
    • Baron W, Decker L, Colognato H, ffrench-Constant C (2003) Regulation of integrin growth factor interactions in oligodendrocytes by lipid raft microdomains. Curr Biol 13: 151-155.
    • (2003) Curr Biol , vol.13 , pp. 151-155
    • Baron, W.1    Decker, L.2    Colognato, H.3    Ffrench-Constant, C.4
  • 58
    • 3042609777 scopus 로고    scopus 로고
    • Lipid rafts: Microenvironments for integrin-growth factor interactions in neural development
    • doi:10.1042/BST0320426
    • Decker L, Baron W, Ffrench-Constant C (2004) Lipid rafts: microenvironments for integrin-growth factor interactions in neural development. Biochem Soc Trans 32: 426-430. doi:10.1042/BST0320426.
    • (2004) Biochem Soc Trans , vol.32 , pp. 426-430
    • Decker, L.1    Baron, W.2    Ffrench-Constant, C.3
  • 59
    • 23944514976 scopus 로고    scopus 로고
    • Human diseases reveal novel roles for neural laminins
    • doi:10.1016/j.tins.2005.07.004
    • Colognato H, ffrench-Constant C, Feltri ML (2005) Human diseases reveal novel roles for neural laminins. Trends Neurosci 28: 480-486. doi:10.1016/j.tins.2005.07.004.
    • (2005) Trends Neurosci , vol.28 , pp. 480-486
    • Colognato, H.1    Ffrench-Constant, C.2    Feltri, M.L.3
  • 60
    • 34249079967 scopus 로고    scopus 로고
    • Reduced raft-association of NF155 in active MS-lesions is accompanied by the disruption of the paranodal junction
    • doi:10.1002/glia.20510
    • Maier O, Baron W, Hoekstra D (2007) Reduced raft-association of NF155 in active MS-lesions is accompanied by the disruption of the paranodal junction. Glia 55: 885-895. doi:10.1002/glia.20510.
    • (2007) Glia , vol.55 , pp. 885-895
    • Maier, O.1    Baron, W.2    Hoekstra, D.3
  • 61
    • 84898030928 scopus 로고    scopus 로고
    • Sulfatide-mediated control of extracellular matrix-dependent oligodendrocyte maturation
    • doi:10.1002/glia.22650
    • Baron W, Bijlard M, Nomden A, de Jonge JC, Teunissen CE, et al. (2014) Sulfatide-mediated control of extracellular matrix-dependent oligodendrocyte maturation. Glia 62: 927-942. doi:10.1002/glia.22650.
    • (2014) Glia , vol.62 , pp. 927-942
    • Baron, W.1    Bijlard, M.2    Nomden, A.3    De Jonge, J.C.4    Teunissen, C.E.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.