메뉴 건너뛰기




Volumn 48, Issue 34, 2009, Pages 8094-8104

Structural polymorphism and multifunctionality of myelin basic protein

Author keywords

[No Author keywords available]

Indexed keywords

BAR-CODES; BIOLOGICAL APPROACH; CENTRAL NERVOUS SYSTEMS; CONFORMATIONAL DYNAMICS; CYTOPLASMIC LEAFLET; CYTOSKELETAL ORGANIZATION; CYTOSKELETONS; CYTOSOLS; DISORDERED PROTEINS; EXTRACELLULAR SIGNALS; HYDROPHOBIC RESIDUES; INTRINSIC DISORDER; ISOFORMS; LARGE EFFECTIVE; MEMBRANE PROCESS; MULTIFUNCTIONALITY; MULTILAMELLAR; MULTILAMELLAR STRUCTURE; MULTIPLE SCLEROSIS; MYELIN BASIC PROTEIN; MYELINATION; NET CHARGES; NEUTRAL PH; OLIGODENDROCYTES; PHYSICOCHEMICAL PROPERTY; POST-TRANSLATIONAL MODIFICATIONS; PROTEIN SURFACE; REMYELINATION; SECONDARY STRUCTURE ELEMENTS; SIGNAL PROPAGATION; SIGNALING NETWORKS; SMALL MOLECULES; STRUCTURAL POLYMORPHISMS; TRANSMEMBRANES;

EID: 69249091013     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi901005f     Document Type: Review
Times cited : (170)

References (92)
  • 1
    • 0035066639 scopus 로고    scopus 로고
    • Biology of oligodendrocyte and myelin in the mammalian central nervous system
    • Baumann, N., and 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
    • 69249129331 scopus 로고    scopus 로고
    • The Properties and Functions of the GOLLI Myelin Basic Proteins
    • Boggs, J. M, Ed, pp, Nova Science Publishers, New York
    • Campagnoni, A. T., and Campagnoni, C. W. (2008) The Properties and Functions of the GOLLI Myelin Basic Proteins, in Myelin Basic Protein (Boggs, J. M., Ed.) pp 1-17, Nova Science Publishers, New York.
    • (2008) Myelin Basic Protein , pp. 1-17
    • Campagnoni, A.T.1    Campagnoni, C.W.2
  • 3
    • 77951787359 scopus 로고    scopus 로고
    • Regulation of store-operated and voltage-operated Ca++ channels in the proliferation and death of oligodendrocyte precursor cells by Golli proteins
    • Paez, P. M., Fulton, D. J., Spreuer, V., Handley, V., Campagnoni, C. W., and Campagnoni, A. T. (2009) Regulation of store-operated and voltage-operated Ca++ channels in the proliferation and death of oligodendrocyte precursor cells by Golli proteins. ASN Neuro 1, e00003.
    • (2009) ASN Neuro , vol.1
    • Paez, P.M.1    Fulton, D.J.2    Spreuer, V.3    Handley, V.4    Campagnoni, C.W.5    Campagnoni, A.T.6
  • 4
    • 69249131573 scopus 로고    scopus 로고
    • The classic basic protein of myelin: Conserved structural motifs and the dynamic molecular barcode involved in membrane adhesion and protein-protein interactions
    • Harauz, G., and Libich, D. S. (2009) The classic basic protein of myelin: Conserved structural motifs and the dynamic molecular barcode involved in membrane adhesion and protein-protein interactions. Curr. Protein Pept. Sci. 10, 196-215.
    • (2009) Curr. Protein Pept. Sci , vol.10 , pp. 196-215
    • Harauz, G.1    Libich, D.S.2
  • 6
    • 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
  • 8
    • 0001331632 scopus 로고    scopus 로고
    • Myelin Basic Protein, The "Executive" Molecule of the Myelin Membrane
    • Juurlink, B. H. J, Devon, R. M, Doucette, J. R, Nazarali, A. J, Schreyer, D. J, and Verge, V. M. K, Eds, pp, Plenum Press, New York
    • Moscarello, M. A. (1997) Myelin Basic Protein, The "Executive" Molecule of the Myelin Membrane, in Cell Biology and Pathology of Myelin: Evolving Biological Concepts and Therapeutic Approaches (Juurlink, B. H. J., Devon, R. M., Doucette, J. R., Nazarali, A. J., Schreyer, D. J., and Verge, V. M. K., Eds.) pp 13-25, Plenum Press, New York.
    • (1997) Cell Biology and Pathology of Myelin: Evolving Biological Concepts and Therapeutic Approaches , pp. 13-25
    • Moscarello, M.A.1
  • 9
    • 0026774285 scopus 로고
    • The basic protein of CNS myelin: Its structure and ligand binding
    • Smith, R. (1992) The basic protein of CNS myelin: its structure and ligand binding. J. Neurochem. 59, 1589-1608.
    • (1992) J. Neurochem , vol.59 , pp. 1589-1608
    • Smith, R.1
  • 10
    • 3042553626 scopus 로고    scopus 로고
    • Myelin basic protein: Diverse conformational states of an intrinsically unstructured protein and its roles in myelin assembly and multiple sclerosis
    • Harauz, G., Ishiyama, N., Hill, C. M. D., Bates, I. R., Libich, D. S., and Farès, C. (2004) Myelin basic protein: Diverse conformational states of an intrinsically unstructured protein and its roles in myelin assembly and multiple sclerosis. Micron 35, 503-542.
    • (2004) Micron , vol.35 , pp. 503-542
    • Harauz, G.1    Ishiyama, N.2    Hill, C.M.D.3    Bates, I.R.4    Libich, D.S.5    Farès, C.6
  • 11
    • 33748487414 scopus 로고    scopus 로고
    • Myelin basic protein: A multifunctional protein
    • Boggs, J. M. (2006) Myelin basic protein: A multifunctional protein. Cell. Mol. Life Sci. 63, 1945-1961.
    • (2006) Cell. Mol. Life Sci , vol.63 , pp. 1945-1961
    • Boggs, J.M.1
  • 12
    • 33846927285 scopus 로고    scopus 로고
    • A tale of two citrullines: Structural and functional aspects of myelin basic protein deimination in health and disease
    • Harauz, G., and Musse, A. A. (2007) A tale of two citrullines: Structural and functional aspects of myelin basic protein deimination in health and disease. Neurochem. Res. 32, 137-158.
    • (2007) Neurochem. Res , vol.32 , pp. 137-158
    • Harauz, G.1    Musse, A.A.2
  • 13
    • 64849102424 scopus 로고    scopus 로고
    • Nova Science Publishers, Hauppauge, NY
    • Boggs, J. M. (2008) Myelin Basic Protein , Nova Science Publishers, Hauppauge, NY.
    • (2008) Myelin Basic Protein
    • Boggs, J.M.1
  • 14
    • 0142234077 scopus 로고    scopus 로고
    • Multiple sclerosis: An important role for post-translational modifications of myelin basic protein in pathogenesis
    • Kim, J. K., Mastronardi, F. G., Wood, D. D., Lubman, D. M., Zand, R., and Moscarello, M. A. (2003) Multiple sclerosis: an important role for post-translational modifications of myelin basic protein in pathogenesis. Mol. Cell. Proteomics 2, 453-462.
    • (2003) Mol. Cell. Proteomics , vol.2 , pp. 453-462
    • Kim, J.K.1    Mastronardi, F.G.2    Wood, D.D.3    Lubman, D.M.4    Zand, R.5    Moscarello, M.A.6
  • 15
  • 16
    • 64749117077 scopus 로고    scopus 로고
    • Deimination of Myelin Basic Protein by PAD Enzymes, and Their Role in Multiple Sclerosis
    • Boggs, J. M, Ed, pp, Nova Science Publishers, New York
    • Mastronardi, F. G., and Moscarello, M. A. (2008) Deimination of Myelin Basic Protein by PAD Enzymes, and Their Role in Multiple Sclerosis, in Myelin Basic Protein (Boggs, J. M., Ed.) pp 31-49, Nova Science Publishers, New York.
    • (2008) Myelin Basic Protein , pp. 31-49
    • Mastronardi, F.G.1    Moscarello, M.A.2
  • 17
    • 0028129521 scopus 로고
    • Myelin basic protein mediates extracellular signals that regulate microtubule stability in oligodendrocyte membrane sheets
    • Dyer, C. A., Philibotte, T. M., Wolf, M. K., and Billings-Gagliardi, S. (1994) Myelin basic protein mediates extracellular signals that regulate microtubule stability in oligodendrocyte membrane sheets. J. Neurosci. Res. 39, 97-107.
    • (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
  • 18
    • 0032840879 scopus 로고    scopus 로고
    • Regulation of myelin basic protein phosphorylation by mitogen-activated protein kinase during increased action potential firing in the hippocampus
    • Atkins, C. M., Yon, M., Groome, N. P., and Sweatt, J. D. (1999) Regulation of myelin basic protein phosphorylation by mitogen-activated protein kinase during increased action potential firing in the hippocampus. J. Neurochem. 73, 1090-1097.
    • (1999) J. Neurochem , vol.73 , pp. 1090-1097
    • Atkins, C.M.1    Yon, M.2    Groome, N.P.3    Sweatt, J.D.4
  • 19
    • 0002025291 scopus 로고
    • Structural Organization of Myelin: Role of Lipid-Protein Interactions Determined in Model Systems
    • Jost, P. C, and Griffith, O. H, Eds, pp, Wiley-Interscience, New York
    • Boggs, J. M., Moscarello, M. A., and Papahadjopoulos, D. (1982) Structural Organization of Myelin: Role of Lipid-Protein Interactions Determined in Model Systems, in Lipid-Protein Interactions (Jost, P. C., and Griffith, O. H., Eds.) pp 1-51, Wiley-Interscience, New York.
    • (1982) Lipid-Protein Interactions , pp. 1-51
    • Boggs, J.M.1    Moscarello, M.A.2    Papahadjopoulos, D.3
  • 20
    • 0023840428 scopus 로고
    • Membrane interactions in nerve myelin: II. Determination of surface charge from biochemical data
    • Inouye, H., and Kirschner, D. A. (1988) Membrane interactions in nerve myelin: II. Determination of surface charge from biochemical data. Biophys. J. 53, 247-260.
    • (1988) Biophys. J , vol.53 , pp. 247-260
    • Inouye, H.1    Kirschner, D.A.2
  • 21
    • 0021802562 scopus 로고
    • Effect of bovine basic protein charge microheterogeneity on protein-induced aggregation of unilamellar vesicles containing a mixture of acidic and neutral phospholipids
    • Cheifetz, S., and Moscarello, M. A. (1985) Effect of bovine basic protein charge microheterogeneity on protein-induced aggregation of unilamellar vesicles containing a mixture of acidic and neutral phospholipids. Biochemistry 24, 1909-1914.
    • (1985) Biochemistry , vol.24 , pp. 1909-1914
    • Cheifetz, S.1    Moscarello, M.A.2
  • 22
    • 0024567052 scopus 로고
    • The isolation, characterization, and lipid-aggregating properties of a citrulline containing myelin basic protein
    • Wood, D. D., and Moscarello, M. A. (1989) The isolation, characterization, and lipid-aggregating properties of a citrulline containing myelin basic protein. J. Biol. Chem. 264, 5121-5127.
    • (1989) J. Biol. Chem , vol.264 , pp. 5121-5127
    • Wood, D.D.1    Moscarello, M.A.2
  • 23
    • 0030929843 scopus 로고    scopus 로고
    • Effect of posttranslational modifications to myelin basic protein on its ability to aggregate acidic lipid vesicles
    • Boggs, J. M., Yip, P. M., Rangaraj, G., and Jo, E. (1997) Effect of posttranslational modifications to myelin basic protein on its ability to aggregate acidic lipid vesicles. Biochemistry 36, 5065-5071.
    • (1997) Biochemistry , vol.36 , pp. 5065-5071
    • Boggs, J.M.1    Yip, P.M.2    Rangaraj, G.3    Jo, E.4
  • 28
    • 0028840507 scopus 로고
    • Aggregation of acidic lipid vesicles by myelin basic protein: Dependence on potassium concentration
    • Jo, E., and Boggs, J. M. (1995) Aggregation of acidic lipid vesicles by myelin basic protein: dependence on potassium concentration. Biochemistry 34, 13705-13716.
    • (1995) Biochemistry , vol.34 , pp. 13705-13716
    • Jo, E.1    Boggs, J.M.2
  • 29
    • 0020614366 scopus 로고
    • Exclusive potassium dependence of the membrane potential in cultured mouse oligodendrocytes
    • Kettenmann, H., Sonnhof, U., and Schachner, M. (1983) Exclusive potassium dependence of the membrane potential in cultured mouse oligodendrocytes. J. Neurosci. 3, 500-505.
    • (1983) J. Neurosci , vol.3 , pp. 500-505
    • Kettenmann, H.1    Sonnhof, U.2    Schachner, M.3
  • 30
    • 4344587249 scopus 로고    scopus 로고
    • pH microdomains in oligodendrocytes
    • Ro, H. A., and Carson, J. H. (2004) pH microdomains in oligodendrocytes. J. Biol. Chem. 279, 37115-37123.
    • (2004) J. Biol. Chem , vol.279 , pp. 37115-37123
    • Ro, H.A.1    Carson, J.H.2
  • 31
    • 0023676661 scopus 로고
    • Zinc ions stabilise the association of basic protein with brain myelin membranes
    • Earl, C., Chantry, A., Mohammad, N., and Glynn, P. (1988) Zinc ions stabilise the association of basic protein with brain myelin membranes. J. Neurochem. 51, 718-724.
    • (1988) J. Neurochem , vol.51 , pp. 718-724
    • Earl, C.1    Chantry, A.2    Mohammad, N.3    Glynn, P.4
  • 32
    • 0026756712 scopus 로고
    • The N terminus of human myelin basic protein consists of C2, C4, C6, and C8 alkyl carboxylic acids
    • Moscarello, M. A., Pang, H., Pace-Asciak, C. R., and Wood, D. D. (1992) The N terminus of human myelin basic protein consists of C2, C4, C6, and C8 alkyl carboxylic acids. J. Biol. Chem. 267, 9779-9782.
    • (1992) J. Biol. Chem , vol.267 , pp. 9779-9782
    • Moscarello, M.A.1    Pang, H.2    Pace-Asciak, C.R.3    Wood, D.D.4
  • 33
    • 0028201372 scopus 로고
    • Acylation of myelin basic protein peptide 1-21 with alkyl carboxylates 2-10 carbons long affects secondary structure and posttranslational modification
    • Costentino, M., Pritzker, L., Boulias, C., and Moscarello, M. A. (1994) Acylation of myelin basic protein peptide 1-21 with alkyl carboxylates 2-10 carbons long affects secondary structure and posttranslational modification. Biochemistry 33, 4155-4162.
    • (1994) Biochemistry , vol.33 , pp. 4155-4162
    • Costentino, M.1    Pritzker, L.2    Boulias, C.3    Moscarello, M.A.4
  • 34
    • 45349095327 scopus 로고    scopus 로고
    • The self-organization of lipids and proteins of myelin at the membrane interface. Molecular factors underlying the microheterogeneity of domain segregation
    • Rosetti, C. M., Maggio, B., and Oliveira, R. G. (2008) The self-organization of lipids and proteins of myelin at the membrane interface. Molecular factors underlying the microheterogeneity of domain segregation. Biochim. Biophys. Acta 1778, 1665-1675.
    • (2008) Biochim. Biophys. Acta , vol.1778 , pp. 1665-1675
    • Rosetti, C.M.1    Maggio, B.2    Oliveira, R.G.3
  • 35
    • 0037066625 scopus 로고    scopus 로고
    • Compositional domain immiscibility in whole myelin monolayers at the air-water interface and Langmuir-Blodgett films
    • Oliveira, R. G., and Maggio, B. (2002) Compositional domain immiscibility in whole myelin monolayers at the air-water interface and Langmuir-Blodgett films. Biochim. Biophys. Acta 1561, 238-250.
    • (2002) Biochim. Biophys. Acta , vol.1561 , pp. 238-250
    • Oliveira, R.G.1    Maggio, B.2
  • 36
    • 0024843641 scopus 로고
    • Selectivity of interaction of phospholipids with bovine spinal cord myelin basic protein studied by spin-label electron spin resonance
    • Sankaram, M. B., Brophy, P. J., and Marsh, D. (1989) Selectivity of interaction of phospholipids with bovine spinal cord myelin basic protein studied by spin-label electron spin resonance. Biochemistry 28, 9699-9707.
    • (1989) Biochemistry , vol.28 , pp. 9699-9707
    • Sankaram, M.B.1    Brophy, P.J.2    Marsh, D.3
  • 37
    • 69249107993 scopus 로고    scopus 로고
    • Boggs, J. M., Bates, I. R., Musse, A. A., and Harauz, G. (2008) Interactions of the 18.5 kDa Myelin Basic Protein with Lipid Bilayers: Studies by Electron Paramagnetic Resonance Spectroscopy and Implications for Generation of Autoimmunity in Multiple Sclerosis, in Myelin Basic Protein (Boggs, J. M., Ed.) pp 105-125, Nova Science Publishers, New York.
    • Boggs, J. M., Bates, I. R., Musse, A. A., and Harauz, G. (2008) Interactions of the 18.5 kDa Myelin Basic Protein with Lipid Bilayers: Studies by Electron Paramagnetic Resonance Spectroscopy and Implications for Generation of Autoimmunity in Multiple Sclerosis, in Myelin Basic Protein (Boggs, J. M., Ed.) pp 105-125, Nova Science Publishers, New York.
  • 38
    • 0041530267 scopus 로고    scopus 로고
    • Membrane-anchoring and charge effects in the interaction of myelin basic protein with lipid bilayers studied by site-directed spin labeling
    • Bates, I. R., Boggs, J. M., Feix, J. B., and Harauz, G. (2003) Membrane-anchoring and charge effects in the interaction of myelin basic protein with lipid bilayers studied by site-directed spin labeling. J. Biol. Chem. 278, 29041-29047.
    • (2003) J. Biol. Chem , vol.278 , pp. 29041-29047
    • Bates, I.R.1    Boggs, J.M.2    Feix, J.B.3    Harauz, G.4
  • 39
    • 1242316993 scopus 로고    scopus 로고
    • An immunodominant epitope of myelin basic protein is an amphipathic alpha-helix
    • Bates, I. R., Feix, J. B., Boggs, J. M., and Harauz, G. (2004) An immunodominant epitope of myelin basic protein is an amphipathic alpha-helix. J. Biol. Chem. 279, 5757-5764.
    • (2004) J. Biol. Chem , vol.279 , pp. 5757-5764
    • Bates, I.R.1    Feix, J.B.2    Boggs, J.M.3    Harauz, G.4
  • 40
    • 33645210449 scopus 로고    scopus 로고
    • Deimination of membrane-bound myelin basic protein in multiple sclerosis exposes an immunodominant epitope
    • Musse, A. A., Boggs, J. M., and Harauz, G. (2006) Deimination of membrane-bound myelin basic protein in multiple sclerosis exposes an immunodominant epitope. Proc. Natl. Acad. Sci. U.S.A. 103, 4422-4427.
    • (2006) Proc. Natl. Acad. Sci. U.S.A , vol.103 , pp. 4422-4427
    • Musse, A.A.1    Boggs, J.M.2    Harauz, G.3
  • 42
    • 45849117986 scopus 로고    scopus 로고
    • Backbone dynamics of the 18.5 kDa isoform of myelin basic protein reveals transient α-helices and a calmodulin-binding site
    • Libich, D. S., and Harauz, G. (2008) Backbone dynamics of the 18.5 kDa isoform of myelin basic protein reveals transient α-helices and a calmodulin-binding site. Biophys. J. 94, 4847-4866.
    • (2008) Biophys. J , vol.94 , pp. 4847-4866
    • Libich, D.S.1    Harauz, G.2
  • 43
    • 41749092789 scopus 로고    scopus 로고
    • Interaction between the C-terminal region of human myelin basic protein and calmodulin: Analysis of complex formation and solution structure
    • Majava, V., Petoukhov, M. V., Hayashi, N., Pirila, P., Svergun, D. I., and Kursula, P. (2008) Interaction between the C-terminal region of human myelin basic protein and calmodulin: analysis of complex formation and solution structure. BMC Struct. Biol. 8, 10.
    • (2008) BMC Struct. Biol , vol.8 , pp. 10
    • Majava, V.1    Petoukhov, M.V.2    Hayashi, N.3    Pirila, P.4    Svergun, D.I.5    Kursula, P.6
  • 44
    • 24944525686 scopus 로고    scopus 로고
    • Two types of detergent-insoluble, glycosphingolipid/cholesterol-rich membrane domains from isolated myelin
    • Arvanitis, D. N., Min, W., Gong, Y., Heng, Y. M., and Boggs, J. M. (2005) Two types of detergent-insoluble, glycosphingolipid/cholesterol-rich membrane domains from isolated myelin. J. Neurochem. 94, 1696-1710.
    • (2005) J. Neurochem , vol.94 , pp. 1696-1710
    • Arvanitis, D.N.1    Min, W.2    Gong, Y.3    Heng, Y.M.4    Boggs, J.M.5
  • 45
    • 33749033095 scopus 로고    scopus 로고
    • Rafts in oligodendrocytes: Evidence and structure-function relationship
    • Gielen, E., Baron, W., Vandeven, M., Steels, P., Hoekstra, D., and Ameloot, M. (2006) Rafts in oligodendrocytes: Evidence and structure-function relationship. Glia 54, 499-512.
    • (2006) Glia , vol.54 , pp. 499-512
    • Gielen, E.1    Baron, W.2    Vandeven, M.3    Steels, P.4    Hoekstra, D.5    Ameloot, M.6
  • 46
    • 33846926110 scopus 로고    scopus 로고
    • White matter rafting: Membrane microdomains in myelin
    • DeBruin, L. S., and Harauz, G. (2007) White matter rafting: Membrane microdomains in myelin. Neurochem. Res. 32, 213-228.
    • (2007) Neurochem. Res , vol.32 , pp. 213-228
    • DeBruin, L.S.1    Harauz, G.2
  • 47
    • 37549007582 scopus 로고    scopus 로고
    • Wrapping it up: The cell biology of myelination
    • Simons, M., and Trotter, J. (2007) Wrapping it up: The cell biology of myelination. Curr. Opin. Neurobiol. 17, 533-540.
    • (2007) Curr. Opin. Neurobiol , vol.17 , pp. 533-540
    • Simons, M.1    Trotter, J.2
  • 48
    • 42549119962 scopus 로고    scopus 로고
    • Distinct endocytic recycling of myelin proteins promotes oligodendroglial membrane remodeling
    • Winterstein, C., Trotter, J., and Krämer-Albers, E. M. (2008) Distinct endocytic recycling of myelin proteins promotes oligodendroglial membrane remodeling. J. Cell Sci. 121, 834-842.
    • (2008) J. Cell Sci , vol.121 , pp. 834-842
    • Winterstein, C.1    Trotter, J.2    Krämer-Albers, E.M.3
  • 49
    • 0035869627 scopus 로고    scopus 로고
    • Protein kinase C and mitogen-activated protein kinase signalling in oligodendrocytes
    • Stariha, R. L., and Kim, S. U. (2001) Protein kinase C and mitogen-activated protein kinase signalling in oligodendrocytes. Microsc. Res. Technol. 52, 680-688.
    • (2001) Microsc. Res. Technol , vol.52 , pp. 680-688
    • Stariha, R.L.1    Kim, S.U.2
  • 51
    • 0036785238 scopus 로고    scopus 로고
    • Myelin proteolipid protein, basic protein, the small isoform of myelin-associated glycoprotein, and p42MAPK are associated in the Triton X-100 extract of central nervous system myelin
    • Arvanitis, D. N., Yang, W., and Boggs, J. M. (2002) Myelin proteolipid protein, basic protein, the small isoform of myelin-associated glycoprotein, and p42MAPK are associated in the Triton X-100 extract of central nervous system myelin. J. Neurosci. Res. 70, 8-23.
    • (2002) J. Neurosci. Res , vol.70 , pp. 8-23
    • Arvanitis, D.N.1    Yang, W.2    Boggs, J.M.3
  • 52
    • 0028140046 scopus 로고
    • Protein and lipid composition of radial component-enriched CNS myelin
    • Karthigasan, J., Kosaras, B., Nguyen, J., and Kirschner, D. A. (1994) Protein and lipid composition of radial component-enriched CNS myelin. J. Neurochem. 62, 1203-1213.
    • (1994) J. Neurochem , vol.62 , pp. 1203-1213
    • Karthigasan, J.1    Kosaras, B.2    Nguyen, J.3    Kirschner, D.A.4
  • 53
    • 0034992321 scopus 로고    scopus 로고
    • Organizing principles of the axoglial apparatus
    • Pedraza, L., Huang, J. K., and Colman, D. R. (2001) Organizing principles of the axoglial apparatus. Neuron 30, 335-344.
    • (2001) Neuron , vol.30 , pp. 335-344
    • Pedraza, L.1    Huang, J.K.2    Colman, D.R.3
  • 54
    • 52949142768 scopus 로고    scopus 로고
    • Myelin basic protein as a "PI(4,5)P2-modulin": A new biological function for a major central nervous system protein
    • Musse, A. A., Gao, W., Homchaudhuri, L., Boggs, J. M., and Harauz, G. (2008) Myelin basic protein as a "PI(4,5)P2-modulin": A new biological function for a major central nervous system protein. Biochemistry 47, 10372-10382.
    • (2008) Biochemistry , vol.47 , pp. 10372-10382
    • Musse, A.A.1    Gao, W.2    Homchaudhuri, L.3    Boggs, J.M.4    Harauz, G.5
  • 55
    • 57549106936 scopus 로고    scopus 로고
    • Myelin basic protein co-distributes with other PI(4,5)P2-sequestering proteins in Triton X-100 detergent-resistant membrane microdomains
    • Musse, A. A., Gao, W., Rangaraj, G., Boggs, J. M., and Harauz, G. (2009) Myelin basic protein co-distributes with other PI(4,5)P2-sequestering proteins in Triton X-100 detergent-resistant membrane microdomains. Neurosci. Lett. 450, 32-36.
    • (2009) Neurosci. Lett , vol.450 , pp. 32-36
    • Musse, A.A.1    Gao, W.2    Rangaraj, G.3    Boggs, J.M.4    Harauz, G.5
  • 56
    • 65549136348 scopus 로고    scopus 로고
    • Phosphatidylinositol 4,5-bisphosphate-dependent interaction of myelin basic protein with the plasma membrane in oligodendroglial cells and its rapid perturbation by elevated calcium
    • Nawaz, S., Kippert, A., Saab, A. S., Werner, H. B., Lang, T., Nave, K. A., and Simons, M. (2009) Phosphatidylinositol 4,5-bisphosphate-dependent interaction of myelin basic protein with the plasma membrane in oligodendroglial cells and its rapid perturbation by elevated calcium. J. Neurosci. 29, 4794-4807.
    • (2009) J. Neurosci , vol.29 , pp. 4794-4807
    • Nawaz, S.1    Kippert, A.2    Saab, A.S.3    Werner, H.B.4    Lang, T.5    Nave, K.A.6    Simons, M.7
  • 57
    • 77950612904 scopus 로고    scopus 로고
    • Myelin Basic Protein Interactions with Actin and Tubulin
    • Boggs, J. M, Ed, pp, Nova Science Publishers, New York
    • Boggs, J. M. (2008) Myelin Basic Protein Interactions with Actin and Tubulin in Vitro: Binding, Assembly, and Regulation, in Myelin Basic Protein (Boggs, J. M., Ed.) pp 149-167, Nova Science Publishers, New York.
    • (2008) Vitro: Binding, Assembly, and Regulation, in Myelin Basic Protein , pp. 149-167
    • Boggs, J.M.1
  • 58
    • 69249100374 scopus 로고    scopus 로고
    • Galiano, M. R., Lopez Sambrooks, and C., Hallak, M. E. (2008) Insights into the Interaction of Myelin Basic Protein with Microtubules, in Myelin Basic Protein (Boggs, J. M., Ed.) pp 129-147, Nova Science Publishers, New York.
    • Galiano, M. R., Lopez Sambrooks, and C., Hallak, M. E. (2008) Insights into the Interaction of Myelin Basic Protein with Microtubules, in Myelin Basic Protein (Boggs, J. M., Ed.) pp 129-147, Nova Science Publishers, New York.
  • 59
    • 15444365811 scopus 로고    scopus 로고
    • MARCKS is a natively unfolded protein with an inaccessible actin-binding site: Evidence for long-range intramolecular interactions
    • Tapp, H., Al-Naggar, I. M., Yarmola, E. G., Harrison, A., Shaw, G., Edison, A. S., and Bubb, M. R. (2005) MARCKS is a natively unfolded protein with an inaccessible actin-binding site: evidence for long-range intramolecular interactions. J. Biol. Chem. 280, 9946-9956.
    • (2005) J. Biol. Chem , vol.280 , pp. 9946-9956
    • Tapp, H.1    Al-Naggar, I.M.2    Yarmola, E.G.3    Harrison, A.4    Shaw, G.5    Edison, A.S.6    Bubb, M.R.7
  • 60
    • 0034604261 scopus 로고    scopus 로고
    • Interaction of lipid-bound myelin basic protein with actin filaments and calmodulin
    • Boggs, J. M., and Rangaraj, G. (2000) Interaction of lipid-bound myelin basic protein with actin filaments and calmodulin. Biochemistry 39, 7799-7806.
    • (2000) Biochemistry , vol.39 , pp. 7799-7806
    • Boggs, J.M.1    Rangaraj, G.2
  • 61
    • 30744479193 scopus 로고    scopus 로고
    • Effect of phosphorylation of myelin basic protein by MAPK on its interactions with actin and actin binding to a lipid membrane in vitro
    • Boggs, J. M., Rangaraj, G., Gao, W., and Heng, Y. M. (2006) Effect of phosphorylation of myelin basic protein by MAPK on its interactions with actin and actin binding to a lipid membrane in vitro. Biochemistry 45, 391-401.
    • (2006) Biochemistry , vol.45 , pp. 391-401
    • Boggs, J.M.1    Rangaraj, G.2    Gao, W.3    Heng, Y.M.4
  • 62
    • 69249134073 scopus 로고    scopus 로고
    • Myelin basic protein binds microtubules to a membrane surface in vitro: Effect of phosphorylation and deimination
    • Boggs, J. M., Rangaraj, G., Heng, Y.-M., and Harauz, G. (2009) Myelin basic protein binds microtubules to a membrane surface in vitro: Effect of phosphorylation and deimination. J. Neurochem. 108 (Suppl 1), 64.
    • (2009) J. Neurochem , vol.108 , Issue.SUPPL. 1 , pp. 64
    • Boggs, J.M.1    Rangaraj, G.2    Heng, Y.-M.3    Harauz, G.4
  • 63
    • 7444270291 scopus 로고    scopus 로고
    • Electron paramagnetic resonance spectroscopy and molecular modelling of the interaction of myelin basic protein (MBP) with calmodulin (CaM)-diversity and conformational adaptability of MBP CaM-targets
    • Polverini, E., Boggs, J. M., Bates, I. R., Harauz, G., and Cavatorta, P. (2004) Electron paramagnetic resonance spectroscopy and molecular modelling of the interaction of myelin basic protein (MBP) with calmodulin (CaM)-diversity and conformational adaptability of MBP CaM-targets. J. Struct. Biol. 148, 353-369.
    • (2004) J. Struct. Biol , vol.148 , pp. 353-369
    • Polverini, E.1    Boggs, J.M.2    Bates, I.R.3    Harauz, G.4    Cavatorta, P.5
  • 64
    • 53049087282 scopus 로고    scopus 로고
    • Amazing stability of phosphate-quaternary amine interactions
    • Woods, A. S., Moyer, S. C., and Jackson, S. N. (2008) Amazing stability of phosphate-quaternary amine interactions. J. Proteome Res. 7, 3423-3427.
    • (2008) J. Proteome Res , vol.7 , pp. 3423-3427
    • Woods, A.S.1    Moyer, S.C.2    Jackson, S.N.3
  • 65
    • 0024327316 scopus 로고
    • Characterization of a cytoskeletal matrix associated with myelin from rat brain
    • Gillespie, C. S., Wilson, R., Davidson, A., and Brophy, P. J. (1989) Characterization of a cytoskeletal matrix associated with myelin from rat brain. Biochem. J. 260, 689-696.
    • (1989) Biochem. J , vol.260 , pp. 689-696
    • Gillespie, C.S.1    Wilson, R.2    Davidson, A.3    Brophy, P.J.4
  • 67
    • 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
    • Boggs, J. M., Gao, W., and 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.
    • (2008) Biochim. Biophys. Acta , vol.1780 , pp. 445-455
    • Boggs, J.M.1    Gao, W.2    Hirahara, Y.3
  • 68
    • 0024320814 scopus 로고
    • Role for the oligodendrocyte cytoskeleton in myelination
    • Wilson, R., and Brophy, P. J. (1989) Role for the oligodendrocyte cytoskeleton in myelination. J. Neurosci. Res. 22, 439-448.
    • (1989) J. Neurosci. Res , vol.22 , pp. 439-448
    • Wilson, R.1    Brophy, P.J.2
  • 69
    • 0024456055 scopus 로고
    • Organization of oligodendroglial membrane sheets: II. Galactocerebroside:antibody interactions signal changes in cytoskeleton and myelin basic protein
    • Dyer, C. A., and Benjamins, J. A. (1989) Organization of oligodendroglial membrane sheets: II. Galactocerebroside:antibody interactions signal changes in cytoskeleton and myelin basic protein. J. Neurosci. Res. 24, 212-221.
    • (1989) J. Neurosci. Res , vol.24 , pp. 212-221
    • Dyer, C.A.1    Benjamins, J.A.2
  • 70
    • 0024442564 scopus 로고
    • Organization of oligodendroglial membrane sheets. I: Association of myelin basic protein and 2′,3′-cyclic nucleotide 3′-phosphohydrolase with cytoskeleton
    • Dyer, C. A., and Benjamins, J. A. (1989) Organization of oligodendroglial membrane sheets. I: Association of myelin basic protein and 2′,3′-cyclic nucleotide 3′-phosphohydrolase with cytoskeleton. J. Neurosci. Res. 24, 201-211.
    • (1989) J. Neurosci. Res , vol.24 , pp. 201-211
    • Dyer, C.A.1    Benjamins, J.A.2
  • 71
    • 69249144738 scopus 로고    scopus 로고
    • Identification of binding partners for the cytoplasmic loop of connexin43: A novel interaction with beta-tubulin
    • Kang, E. Y., Ponzio, M., Gupta, P. P., Liu, F., Butensky, A., and Gutstein, D. E. (2009) Identification of binding partners for the cytoplasmic loop of connexin43: A novel interaction with beta-tubulin. Cell Commun. Adhes. 1-10.
    • (2009) Cell Commun. Adhes , pp. 1-10
    • Kang, E.Y.1    Ponzio, M.2    Gupta, P.P.3    Liu, F.4    Butensky, A.5    Gutstein, D.E.6
  • 72
    • 0028932568 scopus 로고
    • Cytoskeleton in myelin-basic-protein-deficient shiverer oligodendrocytes
    • Dyer, C. A., Philibotte, T. M., Billings-Gagliardi, S., and Wolf, M. K. (1995) Cytoskeleton in myelin-basic-protein-deficient shiverer oligodendrocytes. Dev. Neurosci. 17, 53-62.
    • (1995) Dev. Neurosci , vol.17 , pp. 53-62
    • Dyer, C.A.1    Philibotte, T.M.2    Billings-Gagliardi, S.3    Wolf, M.K.4
  • 73
    • 0030861428 scopus 로고    scopus 로고
    • Regulation of cytoskeleton by myelin components: Studies on shiverer oligodendrocytes carrying an Mbp transgene
    • Dyer, C. A., Phillbotte, T., Wolf, M. K., and Billings-Gagliardi, S. (1997) Regulation of cytoskeleton by myelin components: studies on shiverer oligodendrocytes carrying an Mbp transgene. Dev. Neurosci. 19, 395-409.
    • (1997) Dev. Neurosci , vol.19 , pp. 395-409
    • Dyer, C.A.1    Phillbotte, T.2    Wolf, M.K.3    Billings-Gagliardi, S.4
  • 74
    • 30644473886 scopus 로고    scopus 로고
    • Myelin basic protein, an autoantigen in multiple sclerosis, is selectively processed by human trypsin 4
    • Medveczky, P., Antal, J., Patthy, A., Kekesi, K., Juhasz, G., Szilagyi, L., and Graf, L. (2006) Myelin basic protein, an autoantigen in multiple sclerosis, is selectively processed by human trypsin 4. FEBS Lett. 580, 545-552.
    • (2006) FEBS Lett , vol.580 , pp. 545-552
    • Medveczky, P.1    Antal, J.2    Patthy, A.3    Kekesi, K.4    Juhasz, G.5    Szilagyi, L.6    Graf, L.7
  • 75
    • 37849026077 scopus 로고    scopus 로고
    • Binding of the proline-rich segment of myelin basic protein to SH3-domains: Spectroscopic, microarray, and modelling studies of ligand conformation and effects of post-translational modifications
    • Polverini, E., Rangaraj, G., Libich, D. S., Boggs, J. M., and Harauz, G. (2008) Binding of the proline-rich segment of myelin basic protein to SH3-domains: Spectroscopic, microarray, and modelling studies of ligand conformation and effects of post-translational modifications. Biochemistry 47, 267-282.
    • (2008) Biochemistry , vol.47 , pp. 267-282
    • Polverini, E.1    Rangaraj, G.2    Libich, D.S.3    Boggs, J.M.4    Harauz, G.5
  • 76
    • 64849090288 scopus 로고    scopus 로고
    • Influence of membrane surface charge and post-translational modifications to myelin basic protein on its ability to tether the Fyn-SH3 domain to a membrane in vitro
    • Homchaudhuri, L., Polverini, E., Gao, W., Harauz, G., and Boggs, J. M. (2009) Influence of membrane surface charge and post-translational modifications to myelin basic protein on its ability to tether the Fyn-SH3 domain to a membrane in vitro. Biochemistry 48, 2385-2393.
    • (2009) Biochemistry , vol.48 , pp. 2385-2393
    • Homchaudhuri, L.1    Polverini, E.2    Gao, W.3    Harauz, G.4    Boggs, J.M.5
  • 77
    • 58149214423 scopus 로고    scopus 로고
    • Misincorporation of the proline analog azetidine-2-carboxylic acid in the pathogenesis of multiple sclerosis: A hypothesis
    • Rubenstein, E. (2008) Misincorporation of the proline analog azetidine-2-carboxylic acid in the pathogenesis of multiple sclerosis: a hypothesis. J. Neuropathol. Exp. Neurol. 67, 1035-1040.
    • (2008) J. Neuropathol. Exp. Neurol , vol.67 , pp. 1035-1040
    • Rubenstein, E.1
  • 79
    • 33644945729 scopus 로고    scopus 로고
    • Solution NMR structure of an immunodominant epitope of myelin basic protein. Conformational dependence on environment of an intrinsically unstructured protein
    • Farès, C., Libich, D. S., and Harauz, G. (2006) Solution NMR structure of an immunodominant epitope of myelin basic protein. Conformational dependence on environment of an intrinsically unstructured protein. FEBS J. 273, 601-614.
    • (2006) FEBS J , vol.273 , pp. 601-614
    • Farès, C.1    Libich, D.S.2    Harauz, G.3
  • 80
    • 36849024393 scopus 로고    scopus 로고
    • Solid-state NMR spectroscopy of 18.5 kDa myelin basic protein reconstituted with lipid vesicles: Spectroscopic characterisation and spectral assignments of solvent-exposed protein fragments
    • Zhong, L., Bamm, V. V., Ahmed, M. A., Harauz, G., and Ladizhansky, V. (2007) Solid-state NMR spectroscopy of 18.5 kDa myelin basic protein reconstituted with lipid vesicles: spectroscopic characterisation and spectral assignments of solvent-exposed protein fragments. Biochim. Biophys. Acta 1768, 3193-3205.
    • (2007) Biochim. Biophys. Acta , vol.1768 , pp. 3193-3205
    • Zhong, L.1    Bamm, V.V.2    Ahmed, M.A.3    Harauz, G.4    Ladizhansky, V.5
  • 81
    • 58849142127 scopus 로고    scopus 로고
    • Induced secondary structure and polymorphism in an intrinsically disordered structural linker of the CNS: Solid-state NMR and FTIR spectroscopy of myelin basic protein bound to actin
    • Ahmed, M. A., Bamm, V. V., Shi, L., Steiner-Mosonyi, M., Dawson, J. F., Brown, L., Harauz, G., and Ladizhansky, V. (2009) Induced secondary structure and polymorphism in an intrinsically disordered structural linker of the CNS: Solid-state NMR and FTIR spectroscopy of myelin basic protein bound to actin. Biophys. J. 96, 180-191.
    • (2009) Biophys. J , vol.96 , pp. 180-191
    • Ahmed, M.A.1    Bamm, V.V.2    Shi, L.3    Steiner-Mosonyi, M.4    Dawson, J.F.5    Brown, L.6    Harauz, G.7    Ladizhansky, V.8
  • 82
    • 37749053887 scopus 로고    scopus 로고
    • Fuzzy complexes: Polymorphism and structural disorder in protein-protein interactions
    • Tompa, P., and Fuxreiter, M. (2008) Fuzzy complexes: polymorphism and structural disorder in protein-protein interactions. Trends Biochem. Sci. 33, 2-8.
    • (2008) Trends Biochem. Sci , vol.33 , pp. 2-8
    • Tompa, P.1    Fuxreiter, M.2
  • 83
  • 84
    • 0025316135 scopus 로고
    • Glycolipids and transmembrane signaling: Antibodies to galactocerebroside cause an influx of calcium in oligodendrocytes
    • Dyer, C. A., and Benjamins, J. A. (1990) Glycolipids and transmembrane signaling: antibodies to galactocerebroside cause an influx of calcium in oligodendrocytes. J. Cell Biol. 111, 625-633.
    • (1990) J. Cell Biol , vol.111 , pp. 625-633
    • Dyer, C.A.1    Benjamins, J.A.2
  • 85
    • 0027568112 scopus 로고
    • Novel oligodendrocyte transmembrane signaling systems. Investigations utilizing antibodies as ligands
    • Dyer, C. A. (1993) Novel oligodendrocyte transmembrane signaling systems. Investigations utilizing antibodies as ligands. Mol. Neurobiol. 7, 1-22.
    • (1993) Mol. Neurobiol , vol.7 , pp. 1-22
    • Dyer, C.A.1
  • 86
    • 0024231989 scopus 로고
    • Stimulation of oligodendrocyte differentiation in culture by growth in the presence of a monoclonal antibody to sulfated glycolipid
    • Bansal, R., Gard, A. L., and Pfeiffer, S. E. (1988) Stimulation of oligodendrocyte differentiation in culture by growth in the presence of a monoclonal antibody to sulfated glycolipid. J. Neurosci. Res. 21, 260-267.
    • (1988) J. Neurosci. Res , vol.21 , pp. 260-267
    • Bansal, R.1    Gard, A.L.2    Pfeiffer, S.E.3
  • 87
    • 6044236885 scopus 로고    scopus 로고
    • Carbohydrate-to-carbohydrate interaction, through glycosynapse, as a basis of cell recognition and membrane organization
    • Hakomori, S. (2004) Carbohydrate-to-carbohydrate interaction, through glycosynapse, as a basis of cell recognition and membrane organization. Glycoconjugate J. 21, 125-137.
    • (2004) Glycoconjugate J , vol.21 , pp. 125-137
    • Hakomori, S.1
  • 90
    • 0030981458 scopus 로고    scopus 로고
    • The relationship between developing oligodendrocyte units and maturing axons during myelinogenesis in the anterior medullary velum of neonatal rats
    • Butt, A. M., Ibrahim, M., and Berry, M. (1997) The relationship between developing oligodendrocyte units and maturing axons during myelinogenesis in the anterior medullary velum of neonatal rats. J. Neurocytol. 26, 327-338.
    • (1997) J. Neurocytol , vol.26 , pp. 327-338
    • Butt, A.M.1    Ibrahim, M.2    Berry, M.3
  • 91
    • 0842281441 scopus 로고    scopus 로고
    • Three-dimensional electron microscopic studies of the transitional oligodendrocyte associated with the initial stage of myelination in developing rat hippocampal fimbria
    • Ogawa, T., Suzuki, M., Matoh, K., and Sasaki, K. (2004) Three-dimensional electron microscopic studies of the transitional oligodendrocyte associated with the initial stage of myelination in developing rat hippocampal fimbria. Brain Res. Dev. Brain Res. 148, 207-212.
    • (2004) Brain Res. Dev. Brain Res , vol.148 , pp. 207-212
    • Ogawa, T.1    Suzuki, M.2    Matoh, K.3    Sasaki, K.4
  • 92
    • 0006283636 scopus 로고
    • Development and maturation of central nervous system myelin: Comparison of immunohistochemical localization of proteolipid protein and basic protein in myelin and oligodendrocytes
    • Hartman, B. K., Agrawal, H. C., Agrawal, D., and Kalmbach, S. (1982) Development and maturation of central nervous system myelin: comparison of immunohistochemical localization of proteolipid protein and basic protein in myelin and oligodendrocytes. Proc. Natl. Acad. Sci. U.S.A. 79, 4217-4220.
    • (1982) Proc. Natl. Acad. Sci. U.S.A , vol.79 , pp. 4217-4220
    • Hartman, B.K.1    Agrawal, H.C.2    Agrawal, D.3    Kalmbach, S.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.