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Volumn 2, Issue 1, 2006, Pages 15-21

New observations on the compact myelin proteome

Author keywords

Igsf8; MudPIT; Myelin fractionation; Septin 7; Sirtuin 2

Indexed keywords

BIOLOGICAL MARKER; GUANOSINE TRIPHOSPHATASE; LIPID; MEMBRANE PROTEIN; MYELIN; MYELIN BASIC PROTEIN; MYELIN PROTEIN; PROTEOLIPID PROTEIN; PROTEOME; SEPTIN 7; SIRTUIN; SIRTUIN 2; UNCLASSIFIED DRUG;

EID: 32644483139     PISSN: 1740925X     EISSN: 17410533     Source Type: Journal    
DOI: 10.1017/S1740925X06000068     Document Type: Conference Paper
Times cited : (43)

References (27)
  • 1
    • 24044468693 scopus 로고    scopus 로고
    • Valid data from large-scale proteomics studies
    • Chamrad D. and Meyer H.E. (2005) Valid data from large-scale proteomics studies. Nature Methods 2, 647-648.
    • (2005) Nature Methods , vol.2 , pp. 647-648
    • Chamrad, D.1    Meyer, H.E.2
  • 4
    • 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 T.A., Peles E. et al. (1997) The axonal membrane protein Caspr, a homologue of neurexin IV, is a component of the septate-like paranodal junctions that assemble during myelination. Journal of Cell Biology 139, 1495-1506.
    • (1997) Journal of Cell Biology , vol.139 , pp. 1495-1506
    • Einheber, S.1    Zanazzi, G.2    Ching, W.3    Scherer, S.4    Milner, T.A.5    Peles, E.6
  • 5
    • 24044513966 scopus 로고    scopus 로고
    • Comparative evaluation of mass spectrometry platforms used in large-scale proteomics investigations
    • Elias J.E., Haas W., Faherty B.K. and Gygi S.P. (2005) Comparative evaluation of mass spectrometry platforms used in large-scale proteomics investigations. Nature Methods 2, 667-675.
    • (2005) Nature Methods , vol.2 , pp. 667-675
    • Elias, J.E.1    Haas, W.2    Faherty, B.K.3    Gygi, S.P.4
  • 6
    • 0030245731 scopus 로고    scopus 로고
    • A model for central synaptic functional complex formation based on the differential adhesive specificities of the cadherins
    • Fannon A.M. and Colman D.R. (1996) A model for central synaptic functional complex formation based on the differential adhesive specificities of the cadherins. Neuron 17, 423-434.
    • (1996) Neuron , vol.17 , pp. 423-434
    • Fannon, A.M.1    Colman, D.R.2
  • 7
    • 0028204901 scopus 로고
    • Periaxin, a novel protein of myelinating Schwann cells with a possible role in axonal ensheathment
    • Gillespie C.S., Sherman D.L., Blair G.E. and Brophy P.J. (1994) Periaxin, a novel protein of myelinating Schwann cells with a possible role in axonal ensheathment. Neuron 12, 497-508.
    • (1994) Neuron , vol.12 , pp. 497-508
    • Gillespie, C.S.1    Sherman, D.L.2    Blair, G.E.3    Brophy, P.J.4
  • 8
    • 0032103420 scopus 로고    scopus 로고
    • Subunit composition, protein interactions, and structures of the mammalian brain sec6/8 complex and septin filaments
    • Hsu S.C., Hazuka C.D., Roth R., Foletti D.L., Heuser J. and Scheller R.H. (1998) Subunit composition, protein interactions, and structures of the mammalian brain sec6/8 complex and septin filaments. Neuron 20, 1111-1122.
    • (1998) Neuron , vol.20 , pp. 1111-1122
    • Hsu, S.C.1    Hazuka, C.D.2    Roth, R.3    Foletti, D.L.4    Heuser, J.5    Scheller, R.H.6
  • 9
    • 29144469363 scopus 로고    scopus 로고
    • Glial membranes at the node of ranvier prevent neurite outgrowth
    • Published online 17 November 2005; doi: 10.1126/ science.1118313
    • Huang J.K., Phillips G.R., Roth A.D., Pedraza L., Shan W., Belkaid W. et al. (2005) Glial membranes at the node of ranvier prevent neurite outgrowth. Science. Published online 17 November 2005; doi: 10.1126/ science.1118313.
    • (2005) Science
    • Huang, J.K.1    Phillips, G.R.2    Roth, A.D.3    Pedraza, L.4    Shan, W.5    Belkaid, W.6
  • 10
    • 0035063573 scopus 로고    scopus 로고
    • Novel roles for mammalian septins: From vesicle trafficking to oncogenesis
    • Kartmann B. and Roth D. (2001) Novel roles for mammalian septins: from vesicle trafficking to oncogenesis. Journal of Cell Science 114, 839-844.
    • (2001) Journal of Cell Science , vol.114 , pp. 839-844
    • Kartmann, B.1    Roth, D.2
  • 11
    • 0027424792 scopus 로고
    • A proteolipid protein gene family: Expression in sharks and rays and possible evolution from an ancestral gene encoding a pore-forming polypepticle
    • Kitagawa K., Sinoway M.P., Yang C., Gould R.M. and Colman D.R. (1993) A proteolipid protein gene family: expression in sharks and rays and possible evolution from an ancestral gene encoding a pore-forming polypepticle. 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
  • 12
    • 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. and 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
  • 13
    • 0021177812 scopus 로고
    • A novel myelin-associated glycoprotein defined by a mouse monoclonal antibody
    • Linnington C., Webb M. and Woodhams P.L. (1984) A novel myelin-associated glycoprotein defined by a mouse monoclonal antibody. Journal of Neuroimmunology 6, 387-396.
    • (1984) Journal of Neuroimmunology , vol.6 , pp. 387-396
    • Linnington, C.1    Webb, M.2    Woodhams, P.L.3
  • 15
    • 0027521883 scopus 로고
    • Differential expression of dystrophin, utrophin and dystrophin-associated proteins in peripheral nerve
    • Matsumura K., Yamada H., Shimizu T. and Campbell K.P. (1993) Differential expression of dystrophin, utrophin and dystrophin-associated proteins in peripheral nerve. FEBS Letters 334, 281-285.
    • (1993) FEBS Letters , vol.334 , pp. 281-285
    • Matsumura, K.1    Yamada, H.2    Shimizu, T.3    Campbell, K.P.4
  • 16
    • 0037291214 scopus 로고    scopus 로고
    • The human Sir2 ortholog, SIRT2, is an NAD+-dependent tubulin deacetylase
    • North B.J., Marshall B.L., Borra M.T., Denu J.M. and Verdin E. (2003) The human Sir2 ortholog, SIRT2, is an NAD+-dependent tubulin deacetylase. Molecular Cell 11, 437-444.
    • (2003) Molecular Cell , vol.11 , pp. 437-444
    • North, B.J.1    Marshall, B.L.2    Borra, M.T.3    Denu, J.M.4    Verdin, E.5
  • 17
    • 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 S.M. and Colman D.R. (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    Colman, D.R.4
  • 18
    • 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. Journal of Cell Biology 107, 1561-1573.
    • (1988) Journal of Cell Biology , vol.107 , pp. 1561-1573
    • Ranscht, B.1
  • 19
    • 0023198136 scopus 로고
    • The amino acid sequences of the myelin-associated glycoproteins: Homology to the immunoglobulin gene superfamily
    • Salzer J.L., Holmes W.P. and Colman D.R. (1987) The amino acid sequences of the myelin-associated glycoproteins: homology to the immunoglobulin gene superfamily. Journal of Cell Biology 104, 957-965.
    • (1987) Journal of Cell Biology , vol.104 , pp. 957-965
    • Salzer, J.L.1    Holmes, W.P.2    Colman, D.R.3
  • 20
    • 2642575982 scopus 로고    scopus 로고
    • A barrier to lateral diffusion in the cleavage furrow of dividing mammalian cells
    • Schmidt K. and Nichols B.J. (2004) A barrier to lateral diffusion in the cleavage furrow of dividing mammalian cells. Current Biology 14, 1002-1006.
    • (2004) Current Biology , vol.14 , pp. 1002-1006
    • Schmidt, K.1    Nichols, B.J.2
  • 21
    • 0022531345 scopus 로고
    • On the localization of Thy-1-like immunoreactivity in the rodent and human nervous system
    • Seiger A., Almqvist P., Granholm A.C. and Olson L. (1986) On the localization of Thy-1-like immunoreactivity in the rodent and human nervous system. Medical Biology 64, 109-117.
    • (1986) Medical Biology , vol.64 , pp. 109-117
    • Seiger, A.1    Almqvist, P.2    Granholm, A.C.3    Olson, L.4
  • 22
    • 0034968820 scopus 로고    scopus 로고
    • Specific disruption of a schwann cell dystrophin-related protein complex in a demyelinating neuropathy
    • Sherman D.L., Fabrizi C., Gillespie C.S. and Brophy P.J. (2001) Specific disruption of a schwann cell dystrophin-related protein complex in a demyelinating neuropathy. Neuron 30, 677-687.
    • (2001) Neuron , vol.30 , pp. 677-687
    • Sherman, D.L.1    Fabrizi, C.2    Gillespie, C.S.3    Brophy, P.J.4
  • 23
    • 0025471534 scopus 로고
    • Rapid isolation of metabolically active mitochondria from rat brain and subregions using Percoll density gradient centrifugation
    • Sims N.R. (1990) Rapid isolation of metabolically active mitochondria from rat brain and subregions using Percoll density gradient centrifugation. Journal of Neurochemistry 55, 698-707.
    • (1990) Journal of Neurochemistry , vol.55 , pp. 698-707
    • Sims, N.R.1
  • 24
    • 0034618051 scopus 로고    scopus 로고
    • An oligodendrocyte cell adhesion molecule at the site of assembly of the paranodal axo-glial junction
    • Tait S., Gunn-Moore F., Collinson J.M., Huang J., Lubetzki C., Pedraza L. et al. (2000) An oligodendrocyte cell adhesion molecule at the site of assembly of the paranodal axo-glial junction. Journal of Cell Biology 150, 657-666.
    • (2000) Journal of Cell Biology , vol.150 , pp. 657-666
    • Tait, S.1    Gunn-Moore, F.2    Collinson, J.M.3    Huang, J.4    Lubetzki, C.5    Pedraza, L.6
  • 26
    • 0023678987 scopus 로고
    • Cellular and subcellular distribution of 2′,3′-cyclic nucleotide 3′-phosphodiesterase and its mRNA in the rat central nervous system
    • Trapp B.D., Bernier L., Andrews S.B. and Colman D.R. (1988) Cellular and subcellular distribution of 2′,3′-cyclic nucleotide 3′-phosphodiesterase and its mRNA in the rat central nervous system. Journal of Neurochemistry 51, 859-868.
    • (1988) Journal of Neurochemistry , vol.51 , pp. 859-868
    • Trapp, B.D.1    Bernier, L.2    Andrews, S.B.3    Colman, D.R.4
  • 27
    • 0035106351 scopus 로고    scopus 로고
    • Large-scale analysis of the yeast proteome by multidimensional protein identification technology
    • Washburn M.P., Wolters D. and Yates J.R. 3rd (2001) Large-scale analysis of the yeast proteome by multidimensional protein identification technology. Nature Biotechnology 19, 242-247.
    • (2001) Nature Biotechnology , vol.19 , pp. 242-247
    • Washburn, M.P.1    Wolters, D.2    Yates III, J.R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.