메뉴 건너뛰기




Volumn 136, Issue 1, 2001, Pages 30-45

The effects of deimination of myelin basic protein on structures formed by its interaction with phosphoinositide-containing lipid monolayers

Author keywords

Circular dichroism; Citrulline; Deimination; Electron microscopy; Ganglioside; His tag; Lipid tubules; Multiple sclerosis; Myelin basic protein; Phosphatidylinositol; Phosphoinositide

Indexed keywords

ACTIN BINDING PROTEIN; BINDING PROTEIN; CITRULLINE; EPITOPE; FILAGGRIN; LIPID; MARCKS PROTEIN; MYELIN BASIC PROTEIN; NICKEL COMPLEX; PHOSPHATIDYLINOSITOL 4 PHOSPHATE; PHOSPHATIDYLINOSITOL 4,5 BISPHOSPHATE; PROTEIN ACTA; RECOMBINANT PROTEIN; SODIUM CHLORIDE; UNCLASSIFIED DRUG; VINCULIN;

EID: 0035782680     PISSN: 10478477     EISSN: None     Source Type: Journal    
DOI: 10.1006/jsbi.2001.4421     Document Type: Article
Times cited : (52)

References (75)
  • 1
    • 0015243622 scopus 로고
    • A conformation change induced in the basic encephalitogen by lipids
    • Anthony, J. S., and Moscarello, M. A. (1971) A conformation change induced in the basic encephalitogen by lipids. Biochim. Biophys. Acta 243, 429-433.
    • (1971) Biochim. Biophys. Acta , vol.243 , pp. 429-433
    • Anthony, J.S.1    Moscarello, M.A.2
  • 2
    • 0032562113 scopus 로고    scopus 로고
    • Selective deimination of vimentin in calcium ionophore-induced apoptosis of mouse peritoneal macrophages
    • Asaga, H., Yamada, M., and Senshu, T. (1998) Selective deimination of vimentin in calcium ionophore-induced apoptosis of mouse peritoneal macrophages. Biochem. Biophys. Res. Commun. 243, 641-646.
    • (1998) Biochem. Biophys. Res. Commun. , vol.243 , pp. 641-646
    • Asaga, H.1    Yamada, M.2    Senshu, T.3
  • 3
    • 0033544720 scopus 로고    scopus 로고
    • Crystal structure of the vinculin tail suggests a pathway for activation
    • Bakolitsa, C., de Pereda, J. M., Bagshaw, C. R., Critchley, D. R., and Liddington, R. C. (1999) Crystal structure of the vinculin tail suggests a pathway for activation. Cell 99, 603-613.
    • (1999) Cell , vol.99 , pp. 603-613
    • Bakolitsa, C.1    De Pereda, J.M.2    Bagshaw, C.R.3    Critchley, D.R.4    Liddington, R.C.5
  • 7
    • 0034014119 scopus 로고    scopus 로고
    • Cryoelectron microscopy of protein-lipid complexes of human myelin basic protein charge isomers differing in degree of citrullination
    • Beniac, D. R., Wood, D. D., Palaniyar, N., Ottensmeyer, F. P., Moscarello, M. A., and Harauz, G. (2000) Cryoelectron microscopy of protein-lipid complexes of human myelin basic protein charge isomers differing in degree of citrullination. J. Struct. Biol. 129, 80-95.
    • (2000) J. Struct. Biol. , vol.129 , pp. 80-95
    • Beniac, D.R.1    Wood, D.D.2    Palaniyar, N.3    Ottensmeyer, F.P.4    Moscarello, M.A.5    Harauz, G.6
  • 8
    • 0017595651 scopus 로고
    • Phase separation of acidic and neutral phospholipids induced by human myelin basic protein
    • Boggs, J. M., Moscarello, M. A., and Papahadjopoulos, D. (1977) Phase separation of acidic and neutral phospholipids induced by human myelin basic protein. Biochemistry 16, 5420-5426.
    • (1977) Biochemistry , vol.16 , pp. 5420-5426
    • Boggs, J.M.1    Moscarello, M.A.2    Papahadjopoulos, D.3
  • 9
    • 0002025291 scopus 로고
    • Structural organization of myelin: Role of lipid-protein interactions determined in model systems
    • Jost, P. C., and Griffith, O. H. (Eds.), 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 Jost, P. C., and Griffith, O. H. (Eds.), Lipid-Protein Interactions, vol. 2, pp. 1-51, Wiley-Interscience, New York.
    • (1982) Lipid-Protein Interactions , vol.2 , pp. 1-51
    • Boggs, J.M.1    Moscarello, M.A.2    Papahadjopoulos, D.3
  • 10
    • 0033567008 scopus 로고    scopus 로고
    • Highly deiminated isoform of myelin basic protein isolated from multiple sclerosis brain causes fragmentation of lipid vesicles
    • Boggs, J. M., Rangaraj, G., Koshy, K. M., Ackerley, C., Wood, D. D., and Moscarello, M. A. (1999) Highly deiminated isoform of myelin basic protein isolated from multiple sclerosis brain causes fragmentation of lipid vesicles. J. Neurosci. Res. 57, 529-535.
    • (1999) J. Neurosci. Res. , vol.57 , pp. 529-535
    • Boggs, J.M.1    Rangaraj, G.2    Koshy, K.M.3    Ackerley, C.4    Wood, D.D.5    Moscarello, M.A.6
  • 11
    • 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
  • 12
    • 0021987235 scopus 로고
    • The role of charge microheterogeneity of human myelin basic protein in the formation of phosphatidylglycerol multilayers
    • Brady, G. W., Fein, D. B., Wood, D. D., and Moscarello, M. A. (1985) The role of charge microheterogeneity of human myelin basic protein in the formation of phosphatidylglycerol multilayers. Biochem. Biophys. Res. Commun. 126, 1161-1165.
    • (1985) Biochem. Biophys. Res. Commun. , vol.126 , pp. 1161-1165
    • Brady, G.W.1    Fein, D.B.2    Wood, D.D.3    Moscarello, M.A.4
  • 13
    • 0031024787 scopus 로고    scopus 로고
    • Salt triggered inter-membrane exchange of phospholipids and hemifusion by myelin basic protein
    • Cajal, Y., Boggs, J. M., and Jain, M. (1997) Salt triggered inter-membrane exchange of phospholipids and hemifusion by myelin basic protein. Biochemistry 36, 2566-2576.
    • (1997) Biochemistry , vol.36 , pp. 2566-2576
    • Cajal, Y.1    Boggs, J.M.2    Jain, M.3
  • 14
    • 0030568996 scopus 로고    scopus 로고
    • High-level misincorporation of lysine for arginine at AGA codons in a fusion protein expressed in Escherichia coli
    • Calderone, T. L., Stevens, R. D., and Oas, T. G. (1996) High-level misincorporation of lysine for arginine at AGA codons in a fusion protein expressed in Escherichia coli. J. Mol. Biol. 262, 407-412.
    • (1996) J. Mol. Biol. , vol.262 , pp. 407-412
    • Calderone, T.L.1    Stevens, R.D.2    Oas, T.G.3
  • 15
    • 0016117006 scopus 로고
    • Molecular weight estimation of mouse and guinea-pig myelin basic proteins by polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulphate: Influence of ionic strength
    • Campagnoni, A. T., and Magno, C. S. (1974) Molecular weight estimation of mouse and guinea-pig myelin basic proteins by polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulphate: Influence of ionic strength. J. Neurochem. 23, 887-890.
    • (1974) J. Neurochem. , vol.23 , pp. 887-890
    • Campagnoni, A.T.1    Magno, C.S.2
  • 16
    • 0033545896 scopus 로고    scopus 로고
    • Rapid release and unusual stability of immuno-dominant peptide 45-89 from citrullinated myelin basic protein
    • Cao, L., Goodin, R., Wood, D., Moscarello, M. A., and Whitaker, J. N. (1999) Rapid release and unusual stability of immuno-dominant peptide 45-89 from citrullinated myelin basic protein. Biochemistry 38, 6157-6163.
    • (1999) Biochemistry , vol.38 , pp. 6157-6163
    • Cao, L.1    Goodin, R.2    Wood, D.3    Moscarello, M.A.4    Whitaker, J.N.5
  • 17
    • 0033584956 scopus 로고    scopus 로고
    • Actin and phosphoinositide binding of the ActA protein of the bacterial pathogen Listeria monocytogenes
    • Cicchetti, G., Maurer, P., Wagener, P., and Kocks, C. (1999) Actin and phosphoinositide binding of the ActA protein of the bacterial pathogen Listeria monocytogenes. J. Biol. Chem. 274, 33616-33626.
    • (1999) J. Biol. Chem. , vol.274 , pp. 33616-33626
    • Cicchetti, G.1    Maurer, P.2    Wagener, P.3    Kocks, C.4
  • 18
    • 0003096077 scopus 로고    scopus 로고
    • Myelin proteins as mediators of signal transduction
    • Juurlink, B. H. J., Devon, R. M., Doucette, J. R., Nazarali, A. J., Schreyer, D. J., and Verge, V. M. K. (Eds.), Plenum, New York
    • Dyer, C. A. (1997) Myelin proteins as mediators of signal transduction, in Juurlink, B. H. J., Devon, R. M., Doucette, J. R., Nazarali, A. J., Schreyer, D. J., and Verge, V. M. K. (Eds.), Cell Biology and Pathology of Myelin: Evolving Biological Concepts and Therapeutic Approaches, pp. 69-74, Plenum, New York.
    • (1997) Cell Biology and Pathology of Myelin: Evolving Biological Concepts and Therapeutic Approaches , pp. 69-74
    • Dyer, C.A.1
  • 19
    • 0035144718 scopus 로고    scopus 로고
    • Structure analysis of soluble proteins using electron crystallography
    • Ellis, M. J., and Hebert, H. (2001) Structure analysis of soluble proteins using electron crystallography. Micron 32, 541-550.
    • (2001) Micron , vol.32 , pp. 541-550
    • Ellis, M.J.1    Hebert, H.2
  • 21
    • 0033936369 scopus 로고    scopus 로고
    • Analogous structural motifs in myelin basic protein and in MARCKS
    • Harauz, G., Ishiyama, N., and Bates, I. R. (2000) Analogous structural motifs in myelin basic protein and in MARCKS. Mol. Cell. Biochem. 209, 155-163.
    • (2000) Mol. Cell. Biochem. , vol.209 , pp. 155-163
    • Harauz, G.1    Ishiyama, N.2    Bates, I.R.3
  • 22
    • 0028021882 scopus 로고
    • Pleckstrin homology domains bind to phosphatidylinositol-4,5-bisphosphate
    • Harlan, J. E., Hajduk, P. J., Yoon, H. S., and Fesik, S. W. (1994) Pleckstrin homology domains bind to phosphatidylinositol-4,5-bisphosphate. Nature 371, 168-170.
    • (1994) Nature , vol.371 , pp. 168-170
    • Harlan, J.E.1    Hajduk, P.J.2    Yoon, H.S.3    Fesik, S.W.4
  • 23
    • 0021754420 scopus 로고
    • 2 on membrane interactions in myelin of normal and shiverer mice
    • 2 on membrane interactions in myelin of normal and shiverer mice. Biochim. Biophys. Acta 776, 197-208.
    • (1984) Biochim. Biophys. Acta , vol.776 , pp. 197-208
    • Inouye, H.1    Kirschner, D.A.2
  • 24
    • 0003851694 scopus 로고    scopus 로고
    • M.Sc. thesis, Department of Molecular Biology and Genetics, University of Guelph, Guelph
    • Ishiyama, N. (2000) Electron Crystallography of Myelin Basic Protein, M.Sc. thesis, Department of Molecular Biology and Genetics, University of Guelph, Guelph.
    • (2000) Electron Crystallography of Myelin Basic Protein
    • Ishiyama, N.1
  • 26
    • 0000519448 scopus 로고    scopus 로고
    • Electron microscopy of myelin basic protein (MBP) organized as planar arrays on a lipid monolayer surface: Deimination of MBP hinders its organizational properties
    • Bailey, G. W. (Ed.), Microscopy Soc. of America, Chicago Ridge
    • Ishiyama, N., Matharu, P., Bates, I. R., Wood, D. D., Moscarello, M. A., Viner, N. J., and Harauz, G. (2000) Electron microscopy of myelin basic protein (MBP) organized as planar arrays on a lipid monolayer surface: Deimination of MBP hinders its organizational properties, in Bailey, G. W. (Ed.), Microscopy and Microanalysis 2000, pp. 250-251, Microscopy Soc. of America, Chicago Ridge.
    • (2000) Microscopy and Microanalysis 2000 , pp. 250-251
    • Ishiyama, N.1    Matharu, P.2    Bates, I.R.3    Wood, D.D.4    Moscarello, M.A.5    Viner, N.J.6    Harauz, G.7
  • 27
    • 0032855980 scopus 로고    scopus 로고
    • Controlling cytoskeleton structure by phosphoinositide-protein interactions: Phosphoinositide binding protein domains and effects of lipid packing
    • Janmey, P. A., Xian, W., and Flanagan, L. A. (1999) Controlling cytoskeleton structure by phosphoinositide-protein interactions: Phosphoinositide binding protein domains and effects of lipid packing. Chem. Phys. Lipids 101, 93-107.
    • (1999) Chem. Phys. Lipids , vol.101 , pp. 93-107
    • Janmey, P.A.1    Xian, W.2    Flanagan, L.A.3
  • 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
    • 0032516467 scopus 로고    scopus 로고
    • A conserved motif in the tail domain of vinculin mediates association with and insertion into acidic phospholipid bilayers
    • Johnson, R. P., Niggli, V., Durrer, P., and Craig, S. W. (1998) A conserved motif in the tail domain of vinculin mediates association with and insertion into acidic phospholipid bilayers. Biochemistry 37, 10211-10222.
    • (1998) Biochemistry , vol.37 , pp. 10211-10222
    • Johnson, R.P.1    Niggli, V.2    Durrer, P.3    Craig, S.W.4
  • 30
    • 0017720727 scopus 로고
    • Localization of sites for ionic interaction with lipid in the C-terminal third of the bovine myelin basic protein
    • Jones, A. J., and Rumsby, M. G. (1977) Localization of sites for ionic interaction with lipid in the C-terminal third of the bovine myelin basic protein. Biochem. J. 167, 583-591.
    • (1977) Biochem. J. , vol.167 , pp. 583-591
    • Jones, A.J.1    Rumsby, M.G.2
  • 31
    • 0023819170 scopus 로고
    • Phosphatidic acid and phosphoinositide turnover in myelin and its stimulation by acetylcholine
    • Kahn, D. W., and Morell, P. (1988) Phosphatidic acid and phosphoinositide turnover in myelin and its stimulation by acetylcholine. J. Neurochem. 50, 1542-1550.
    • (1988) J. Neurochem. , vol.50 , pp. 1542-1550
    • Kahn, D.W.1    Morell, P.2
  • 32
    • 0018743184 scopus 로고
    • Circular dichroic analysis of the secondary structure of myelin basic protein and derived peptides bound to detergents and to lipid vesicles
    • Keniry, M. A., and Smith, R. (1979) Circular dichroic analysis of the secondary structure of myelin basic protein and derived peptides bound to detergents and to lipid vesicles. Biochim. Biophys. Acta 578, 381-391.
    • (1979) Biochim. Biophys. Acta , vol.578 , pp. 381-391
    • Keniry, M.A.1    Smith, R.2
  • 33
    • 0028590161 scopus 로고
    • Two-dimensional crystallization of histidine-tagged, HIV-1 reverse transcriptase promoted by a novel nickel-chelating lipid
    • Kubalek, E. W., Le Grice, S. F., and Brown, P. O. (1994) Two-dimensional crystallization of histidine-tagged, HIV-1 reverse transcriptase promoted by a novel nickel-chelating lipid. J. Struct. Biol. 113, 117-123.
    • (1994) J. Struct. Biol. , vol.113 , pp. 117-123
    • Kubalek, E.W.1    Le Grice, S.F.2    Brown, P.O.3
  • 34
    • 0032975218 scopus 로고    scopus 로고
    • Modulation of nanotube formation by structural modifications of sphingolipids
    • Kulkarni, V. S., Boggs, J. M., and Brown, R. E. (1999) Modulation of nanotube formation by structural modifications of sphingolipid. Biophys. J. 77, 319-330.
    • (1999) Biophys. J. , vol.77 , pp. 319-330
    • Kulkarni, V.S.1    Boggs, J.M.2    Brown, R.E.3
  • 35
    • 0027317616 scopus 로고
    • Deimination of human myelin basic protein by a peptidylarginine deiminase from bovine brain
    • Lamensa, J. W. E., and Moscarello, M. A. (1993) Deimination of human myelin basic protein by a peptidylarginine deiminase from bovine brain. J. Neurochem. 61, 987-996.
    • (1993) J. Neurochem. , vol.61 , pp. 987-996
    • Lamensa, J.W.E.1    Moscarello, M.A.2
  • 37
    • 0034657147 scopus 로고    scopus 로고
    • Redistribution of cholesterol in oligodendrocyte membrane sheets after activation of distinct signal transduction pathways
    • Lintner, R. N., and Dyer, C. A. (2000) Redistribution of cholesterol in oligodendrocyte membrane sheets after activation of distinct signal transduction pathways. J. Neurosci. Res. 60, 437-449.
    • (2000) J. Neurosci. Res. , vol.60 , pp. 437-449
    • Lintner, R.N.1    Dyer, C.A.2
  • 38
    • 0003076337 scopus 로고
    • Myelin basic protein: What does it do?
    • Kumar, S. (Ed.), Pergamon Press, Oxford
    • Martenson, R. E. (1980) Myelin basic protein: What does it do? in Kumar, S. (Ed.), Biochemistry of Brain, pp. 49-79, Pergamon Press, Oxford.
    • (1980) Biochemistry of Brain , pp. 49-79
    • Martenson, R.E.1
  • 39
    • 0029878653 scopus 로고    scopus 로고
    • Myelin basic protein in experimental allergic encephalomyelitis is not affected at the post-translational level: Implications for demyelinating disease
    • Mastronardi, F. G., Al-Sabbagh, A., Nelson, P. A., Rego, J., Roots, B. I., and Moscarello, M. A. (1996) Myelin basic protein in experimental allergic encephalomyelitis is not affected at the post-translational level: Implications for demyelinating disease. J. Neurosci. Res. 44, 344-349.
    • (1996) J. Neurosci. Res. , vol.44 , pp. 344-349
    • Mastronardi, F.G.1    Al-Sabbagh, A.2    Nelson, P.A.3    Rego, J.4    Roots, B.I.5    Moscarello, M.A.6
  • 40
    • 0032562547 scopus 로고    scopus 로고
    • Phosphatidylinositol and inositol involvement in Alzheimer amyloid-β fibril growth and arrest
    • McLaurin, J., Franklin, T., Chakrabartty, A., and Fraser, P. E. (1998) Phosphatidylinositol and inositol involvement in Alzheimer amyloid-β fibril growth and arrest. J. Mol. Biol. 278, 183-194.
    • (1998) J. Mol. Biol. , vol.278 , pp. 183-194
    • McLaurin, J.1    Franklin, T.2    Chakrabartty, A.3    Fraser, P.E.4
  • 41
    • 0025297420 scopus 로고
    • Myelin basic protein does not contain a phosphatidylinositol anchor
    • McLaurin, J., Hew, C., and Moscarello, M. A. (1990) Myelin basic protein does not contain a phosphatidylinositol anchor. Biochem. J. 269, 278-279.
    • (1990) Biochem. J. , vol.269 , pp. 278-279
    • McLaurin, J.1    Hew, C.2    Moscarello, M.A.3
  • 42
    • 0033863798 scopus 로고    scopus 로고
    • Review: Modulating factors in amyloid-β fibril formation
    • McLaurin, J., Yang, D.-S., Yip, C. M., and Fraser, P. E. (2000) Review: Modulating factors in amyloid-β fibril formation. J. Struct. Biol. 130, 259-270.
    • (2000) J. Struct. Biol. , vol.130 , pp. 259-270
    • McLaurin, J.1    Yang, D.-S.2    Yip, C.M.3    Fraser, P.E.4
  • 43
    • 0000764856 scopus 로고
    • Effect of urea on hydrophobic interaction: Raman difference spectroscopy on C-H stretching vibration of acetone and C-N stretching vibration of urea
    • Mizutani, Y., Kanagawa, K., and Nakanishi, K. (1989) Effect of urea on hydrophobic interaction: Raman difference spectroscopy on C-H stretching vibration of acetone and C-N stretching vibration of urea. J. Phys. Chem. 93, 5650-5654.
    • (1989) J. Phys. Chem. , vol.93 , pp. 5650-5654
    • Mizutani, Y.1    Kanagawa, K.2    Nakanishi, K.3
  • 44
    • 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.), Plenum, New York
    • Moscarello, M. A. (1997) Myelin basic protein, the "executive" molecule of the myelin membrane, in Juurlink, B. H. J., Devon, R. M., Doucette, J. R., Nazarali, A. J., Schreyer, D. J., and Verge, V. M. K. (Eds.), Cell Biology and Pathology of Myelin: Evolving Biological Concepts and Therapeutic Approaches, pp. 13-25, Plenum, New York.
    • (1997) Cell Biology and Pathology of Myelin: Evolving Biological Concepts and Therapeutic Approaches , pp. 13-25
    • Moscarello, M.A.1
  • 46
    • 0035141545 scopus 로고    scopus 로고
    • Two-dimensional crystallogenesis of transmembrane proteins
    • Mosser, G. (2001) Two-dimensional crystallogenesis of transmembrane proteins. Micron 32, 517-540.
    • (2001) Micron , vol.32 , pp. 517-540
    • Mosser, G.1
  • 47
    • 0033059346 scopus 로고    scopus 로고
    • Force measurements on myelin basic protein adsorbed to mica and lipid bilayer surfaces done with the atomic force microscope
    • Mueller, H., Butt, H.-J., and Bamberg, E. (1999) Force measurements on myelin basic protein adsorbed to mica and lipid bilayer surfaces done with the atomic force microscope. Biophys. J. 76, 1072-1079.
    • (1999) Biophys. J. , vol.76 , pp. 1072-1079
    • Mueller, H.1    Butt, H.-J.2    Bamberg, E.3
  • 48
    • 0014127482 scopus 로고
    • Preservation of myelin lamellar structure in the absence of lipid: A correlated chemical and morphological study
    • Napolitano, L., Lebaron, F., and Scaletti, F. (1967) Preservation of myelin lamellar structure in the absence of lipid: A correlated chemical and morphological study. J. Cell Biol. 34, 817-826.
    • (1967) J. Cell Biol. , vol.34 , pp. 817-826
    • Napolitano, L.1    Lebaron, F.2    Scaletti, F.3
  • 50
    • 0011821254 scopus 로고
    • Electron donor-acceptor properties of urea and its role in charge-transfer chromatography
    • Ochoa, J. L., Porath, J., Kempf, J., and Egly, J. M. (1980) Electron donor-acceptor properties of urea and its role in charge-transfer chromatography. J. Chromatogr. 188, 257-261.
    • (1980) J. Chromatogr. , vol.188 , pp. 257-261
    • Ochoa, J.L.1    Porath, J.2    Kempf, J.3    Egly, J.M.4
  • 51
    • 0035782864 scopus 로고    scopus 로고
    • Atomic force microscopy of nonhydroxy galactocerebroside nanotubes and their self-assembly at the air-water interface, with applications to myelin
    • Ohler, B., Revenko, I., and Husted, C. (2001) Atomic force microscopy of nonhydroxy galactocerebroside nanotubes and their self-assembly at the air-water interface, with applications to myelin. J. Struct. Biol. 133, 1-9.
    • (2001) J. Struct. Biol. , vol.133 , pp. 1-9
    • Ohler, B.1    Revenko, I.2    Husted, C.3
  • 52
    • 0032974494 scopus 로고    scopus 로고
    • Conformation of bovine myelin basic protein purified with bound lipids
    • Polverini, E., Fasano, A., Zito, F., Riccio, P., and Cavatorta, P. (1999) Conformation of bovine myelin basic protein purified with bound lipids. Eur. Biophys. J. 28, 351-355.
    • (1999) Eur. Biophys. J. , vol.28 , pp. 351-355
    • Polverini, E.1    Fasano, A.2    Zito, F.3    Riccio, P.4    Cavatorta, P.5
  • 53
    • 0034625091 scopus 로고    scopus 로고
    • Deimination of myelin basic protein. I. The effect of deimination of arginyl residues of MBP on its structure and susceptibility to digestion by cathepsin D
    • Pritzker, L. B., Joshi, S., Gowan, J. J., Harauz, G., and Moscarello, M. A. (2000a) Deimination of myelin basic protein. I. The effect of deimination of arginyl residues of MBP on its structure and susceptibility to digestion by cathepsin D. Biochemistry 39, 5374-5381.
    • (2000) Biochemistry , vol.39 , pp. 5374-5381
    • Pritzker, L.B.1    Joshi, S.2    Gowan, J.J.3    Harauz, G.4    Moscarello, M.A.5
  • 54
    • 0034625146 scopus 로고    scopus 로고
    • Deimination of myelin basic protein. II. The effect of methylation of MBP on its deimination by peptidylarginine deiminase
    • Pritzker, L. B., Joshi, S., Harauz, G., and Moscarello, M. A. (2000b) Deimination of myelin basic protein. II. The effect of methylation of MBP on its deimination by peptidylarginine deiminase. Biochemistry 39, 5382-5388.
    • (2000) Biochemistry , vol.39 , pp. 5382-5388
    • Pritzker, L.B.1    Joshi, S.2    Harauz, G.3    Moscarello, M.A.4
  • 56
    • 0031052088 scopus 로고    scopus 로고
    • Three-dimensional structure of myelin basic protein. II. Molecular modelling and considerations of predicted structures in multiple sclerosis
    • Ridsdale, R. A., Beniac, D. R., Tompkins, T. A., Moscarello, M. A., and Harauz, G. (1997) Three-dimensional structure of myelin basic protein. II. Molecular modelling and considerations of predicted structures in multiple sclerosis. J. Biol. Chem. 272, 4269-4275.
    • (1997) J. Biol. Chem. , vol.272 , pp. 4269-4275
    • Ridsdale, R.A.1    Beniac, D.R.2    Tompkins, T.A.3    Moscarello, M.A.4    Harauz, G.5
  • 57
    • 0029086411 scopus 로고
    • Evidence for sodium dodecyl sulfate/protein complexes adopting a necklace structure
    • Samsó, M., Daban, J.-R., Hansen, S., and Jones, G. R. (1995) Evidence for sodium dodecyl sulfate/protein complexes adopting a necklace structure. Eur. J. Biochem. 232, 818-824.
    • (1995) Eur. J. Biochem. , vol.232 , pp. 818-824
    • Samsó, M.1    Daban, J.-R.2    Hansen, S.3    Jones, G.R.4
  • 59
    • 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
  • 60
    • 0030040708 scopus 로고    scopus 로고
    • Membrane adhesion and other functions for the myelin basic proteins
    • Staugaitis, S. M., Colman, D. R., and Pedraza, L. (1996) Membrane adhesion and other functions for the myelin basic proteins. BioEssays 18, 13-18.
    • (1996) BioEssays , vol.18 , pp. 13-18
    • Staugaitis, S.M.1    Colman, D.R.2    Pedraza, L.3
  • 61
    • 0017151884 scopus 로고
    • Lipid-protein interactions with native and modified myelin basic protein
    • Steck, A. J., Siegrist, H. P., Zahler, P., and Herschkowitz, N. N. (1976) Lipid-protein interactions with native and modified myelin basic protein. Biochim. Biophys. Acta 455, 343-352.
    • (1976) Biochim. Biophys. Acta , vol.455 , pp. 343-352
    • Steck, A.J.1    Siegrist, H.P.2    Zahler, P.3    Herschkowitz, N.N.4
  • 62
    • 0029871758 scopus 로고    scopus 로고
    • Mitosis-specific phosphorylation of vimentin by protein kinase C coupled with reorganization of intracellular membranes
    • Takai, Y., Ogawara, M., Tomono, Y., Moritoh, C., Imajoh-Ohmi, S., Tsutsumi, O., Taketani, Y., and Inagaki, M. (1996) Mitosis-specific phosphorylation of vimentin by protein kinase C coupled with reorganization of intracellular membranes. J. Cell Biol. 133, 141-149.
    • (1996) J. Cell Biol. , vol.133 , pp. 141-149
    • Takai, Y.1    Ogawara, M.2    Tomono, Y.3    Moritoh, C.4    Imajoh-Ohmi, S.5    Tsutsumi, O.6    Taketani, Y.7    Inagaki, M.8
  • 63
    • 0030784777 scopus 로고    scopus 로고
    • The fate of trichohyalin: Sequential post-translational modifications by peptidylarginine deiminase and transglutaminases
    • Tarcsa, E., Marekov, N., Andreoli, J., Idler, W. W., Candi, E., Chung, S. I., and Steinert, P. M. (1997) The fate of trichohyalin: Sequential post-translational modifications by peptidylarginine deiminase and transglutaminases. J. Biol. Chem. 272, 27893-27901.
    • (1997) J. Biol. Chem. , vol.272 , pp. 27893-27901
    • Tarcsa, E.1    Marekov, N.2    Andreoli, J.3    Idler, W.W.4    Candi, E.5    Chung, S.I.6    Steinert, P.M.7
  • 64
    • 0029824853 scopus 로고    scopus 로고
    • Protein unfolding by peptidylarginine deiminase: Substrate specificity and structural relationships of the natural substrates trichohyalin and filaggrin
    • Tarcsa, E., Marekov, N., Mei, G., Melino, G., Lee, S.-C., and Steinert, P. M. (1996) Protein unfolding by peptidylarginine deiminase: Substrate specificity and structural relationships of the natural substrates trichohyalin and filaggrin. J. Biol. Chem. 271, 30709-30716.
    • (1996) J. Biol. Chem. , vol.271 , pp. 30709-30716
    • Tarcsa, E.1    Marekov, N.2    Mei, G.3    Melino, G.4    Lee, S.-C.5    Steinert, P.M.6
  • 65
    • 0026506363 scopus 로고
    • Formation of 2-D paracrystals of F-actin on phospholipid layers mixed with quarternary ammonium surfactants
    • Taylor, K. A., and Taylor, D. W. (1992) Formation of 2-D paracrystals of F-actin on phospholipid layers mixed with quarternary ammonium surfactants. J. Struct. Biol. 108, 140-147.
    • (1992) J. Struct. Biol. , vol.108 , pp. 140-147
    • Taylor, K.A.1    Taylor, D.W.2
  • 66
    • 0033845902 scopus 로고    scopus 로고
    • Enhanced T cell responsiveness to citrulline-containing myelin basic protein in multiple sclerosis patients
    • Tranquill, L. R., Cao, L., Ling, N. C., Kalbacher, H., Martin, R. M., and Whitaker, J. N. (2000) Enhanced T cell responsiveness to citrulline-containing myelin basic protein in multiple sclerosis patients. Mult. Scler. 6, 220-225.
    • (2000) Mult. Scler. , vol.6 , pp. 220-225
    • Tranquill, L.R.1    Cao, L.2    Ling, N.C.3    Kalbacher, H.4    Martin, R.M.5    Whitaker, J.N.6
  • 68
    • 0034467062 scopus 로고    scopus 로고
    • Citrullination: A small change for a protein with great consequences for rheumatoid arthritis
    • van Venrooij, W. J., and Pruijn, G. J. (2000) Citrullination: A small change for a protein with great consequences for rheumatoid arthritis. Arthritis Res. 2, 249-251.
    • (2000) Arthritis Res. , vol.2 , pp. 249-251
    • Van Venrooij, W.J.1    Pruijn, G.J.2
  • 69
    • 0032758723 scopus 로고    scopus 로고
    • The effect of pH on the structure, binding, and model membrane lysis by cecropin B and analogs
    • Wang, W., Smith, K. M., and Chen, H. M. (1999) The effect of pH on the structure, binding, and model membrane lysis by cecropin B and analogs. Biochim. Biophys. Acta 1473, 418-443.
    • (1999) Biochim. Biophys. Acta , vol.1473 , pp. 418-443
    • Wang, W.1    Smith, K.M.2    Chen, H.M.3
  • 71
    • 0029927069 scopus 로고    scopus 로고
    • Acute multiple sclerosis (Marburg type) is associated with extensive modifications of myelin basic protein
    • Wood, D. D., Bilbao, J. M., O'Connors, P., and Moscarello, M. A. (1996) Acute multiple sclerosis (Marburg type) is associated with extensive modifications of myelin basic protein. Ann. Neurol. 40, 18-24.
    • (1996) Ann. Neurol. , vol.40 , pp. 18-24
    • Wood, D.D.1    Bilbao, J.M.2    O'Connors, P.3    Moscarello, M.A.4
  • 72
    • 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
  • 73
    • 0001823237 scopus 로고    scopus 로고
    • Molecular biology of the glia: Components of myelin - Myelin basic protein - The implication of post-translational changes for demyelinating disease
    • Russell, W. (Ed.), Wiley, Chichester/New York
    • Wood, D. D., and Moscarello, M. A. (1997) Molecular biology of the glia: Components of myelin - Myelin basic protein - The implication of post-translational changes for demyelinating disease, in Russell, W. (Ed.), The Molecular Biology of Multiple Sclerosis, pp. 37-54, Wiley, Chichester/New York.
    • (1997) The Molecular Biology of Multiple Sclerosis , pp. 37-54
    • Wood, D.D.1    Moscarello, M.A.2
  • 74
    • 0032727419 scopus 로고    scopus 로고
    • Construct for high-level expression and low misincorporation of lysine for arginine during expression of pET-encoded eukaryotic proteins in Escherichia coli
    • You, J., Cohen, R. E., and Pickart, C. M. (1999) Construct for high-level expression and low misincorporation of lysine for arginine during expression of pET-encoded eukaryotic proteins in Escherichia coli. Biotechniques 27, 950-954.
    • (1999) Biotechniques , vol.27 , pp. 950-954
    • You, J.1    Cohen, R.E.2    Pickart, C.M.3
  • 75
    • 0032562138 scopus 로고    scopus 로고
    • Determination of the sites of posttranslational modifications in the charge isomers of bovine myelin basic protein by capillary electrophoresis-mass spectroscopy
    • Zand, R., Li, M. X., Jin, X., and Lubman, D. (1998) Determination of the sites of posttranslational modifications in the charge isomers of bovine myelin basic protein by capillary electrophoresis-mass spectroscopy. Biochemistry 24, 2441-2449.
    • (1998) Biochemistry , vol.24 , pp. 2441-2449
    • Zand, R.1    Li, M.X.2    Jin, X.3    Lubman, D.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.