메뉴 건너뛰기




Volumn 21, Issue 4, 1996, Pages 527-535

Phosphorylation of myelin proteins: Recent advances

Author keywords

myelin assembly; myelin proteins; phosphoamino acids; Phosphorylation; protein kinases; signal transduction

Indexed keywords

2',3' CYCLIC NUCLEOTIDE 3' PHOSPHODIESTERASE; CYCLIC AMP DEPENDENT PROTEIN KINASE; MITOGEN ACTIVATED PROTEIN KINASE; MYELIN ASSOCIATED GLYCOPROTEIN; MYELIN BASIC PROTEIN; MYELIN PROTEIN; PROTEIN KINASE; PROTEIN KINASE (CALCIUM,CALMODULIN); PROTEIN KINASE C; GLYCOPROTEIN;

EID: 0029666456     PISSN: 03643190     EISSN: None     Source Type: Journal    
DOI: 10.1007/BF02527718     Document Type: Short Survey
Times cited : (42)

References (84)
  • 1
    • 0015240537 scopus 로고
    • Phosphorylation of endogenous proteins of rat brain by cyclic adenosine 3′5′-cyclic monophosphate-dependent protein kinase
    • Johnson, E. M., Maeno, H., and Greengard, P. 1971. Phosphorylation of endogenous proteins of rat brain by cyclic adenosine 3′5′-cyclic monophosphate-dependent protein kinase. J. Biol. Chem. 246:7731-7739.
    • (1971) J. Biol. Chem. , vol.246 , pp. 7731-7739
    • Johnson, E.M.1    Maeno, H.2    Greengard, P.3
  • 2
    • 0016150422 scopus 로고
    • In vitro and in vivo phosphorylation of myelin basic protein by endogenous and exogenous adenosine 3′5′-cyclic monophosphate-dependent protein kinase in brain
    • Miyamoto, E., and Kakuichi, S. 1974. In vitro and in vivo phosphorylation of myelin basic protein by endogenous and exogenous adenosine 3′5′-cyclic monophosphate-dependent protein kinase in brain. J. Biol. Chem. 249:2769-2777.
    • (1974) J. Biol. Chem. , vol.249 , pp. 2769-2777
    • Miyamoto, E.1    Kakuichi, S.2
  • 3
    • 0023779256 scopus 로고
    • The phosphorylation of myelin proteins
    • Ulmer, J. B. 1988. The phosphorylation of myelin proteins. Prog. Neurobiol. 31:241-259.
    • (1988) Prog. Neurobiol. , vol.31 , pp. 241-259
    • Ulmer, J.B.1
  • 4
    • 0002726230 scopus 로고
    • Enzymes and receptors of myelin
    • Martenson, R. E. (ed) CRC Press, Boca Raton, FL
    • Ledeen, R. W. 1992. Enzymes and receptors of myelin. Pages 531-570, in Martenson, R. E. (ed) Myelin, Biology and Chemistry CRC Press, Boca Raton, FL.
    • (1992) Myelin, Biology and Chemistry , pp. 531-570
    • Ledeen, R.W.1
  • 5
    • 0015890189 scopus 로고
    • Phosphorylation of myelin basic protein by an adenosine 3′,5′-cyclic monophosphate dependent protein kinase
    • Carnegie, P. R., Dunkley, P. R., Kemp, B. E., and Murray, A. W. 1973. Phosphorylation of myelin basic protein by an adenosine 3′,5′-cyclic monophosphate dependent protein kinase. Biochem. J. 135:569-572.
    • (1973) Biochem. J. , vol.135 , pp. 569-572
    • Carnegie, P.R.1    Dunkley, P.R.2    Kemp, B.E.3    Murray, A.W.4
  • 6
    • 0020429526 scopus 로고
    • Basic protein in brain myelin is phosphorylated by endogenous phospholipid-sensitive calcium-dependent protein kinase
    • Turner, R. S., Chou, C.-H. J., Kibler, R. F., and Kuo, J. 1982. Basic protein in brain myelin is phosphorylated by endogenous phospholipid-sensitive calcium-dependent protein kinase. J. Neurochem. 39:1397-1404.
    • (1982) J. Neurochem. , vol.39 , pp. 1397-1404
    • Turner, R.S.1    Chou, C.-H.J.2    Kibler, R.F.3    Kuo, J.4
  • 7
    • 0021518943 scopus 로고
    • Phospholipid-sensitive calcium-dependent protein kinase preferentially phosphorylates serine-115 of bovine myelin basic protein
    • Turner, R. S., Chou, C.-H. J., Mazzei, G. J., Bembure, P., and Kuo, J. F. 1984. Phospholipid-sensitive calcium-dependent protein kinase preferentially phosphorylates serine-115 of bovine myelin basic protein. J. Neurochem. 43:1257-1264.
    • (1984) J. Neurochem. , vol.43 , pp. 1257-1264
    • Turner, R.S.1    Chou, C.-H.J.2    Mazzei, G.J.3    Bembure, P.4    Kuo, J.F.5
  • 8
    • 0022348840 scopus 로고
    • Studies on the phosphorylation of myelin basic protein by protein kinase C and adenosine 3′,5′-monophosphate dependent protein kinase
    • Kishimoto, A., Nishiyama, K., Nakanishi, H., Uratsuji, Y., Nomura, H., Takeyama, Y., and Nishizuka, Y. 1985. Studies on the phosphorylation of myelin basic protein by protein kinase C and adenosine 3′,5′-monophosphate dependent protein kinase. J. Biol. Chem. 260:12492-12499.
    • (1985) J. Biol. Chem. , vol.260 , pp. 12492-12499
    • Kishimoto, A.1    Nishiyama, K.2    Nakanishi, H.3    Uratsuji, Y.4    Nomura, H.5    Takeyama, Y.6    Nishizuka, Y.7
  • 9
    • 0022723585 scopus 로고
    • Activation of myelin protein kinase by diacylglycerol and 4 beta-phorbol-12-myristate-13-acetate
    • Murray, N., and Steck, A. J. 1986. Activation of myelin protein kinase by diacylglycerol and 4 beta-phorbol-12-myristate-13-acetate. J. Neurochem. 46:1655-1657.
    • (1986) J. Neurochem. , vol.46 , pp. 1655-1657
    • Murray, N.1    Steck, A.J.2
  • 10
  • 12
    • 0022929851 scopus 로고
    • A) as a myelin basic protein kinase in the brain
    • A) as a myelin basic protein kinase in the brain. J. Biol. Chem. 261:11786-11791.
    • (1986) J. Biol. Chem. , vol.261 , pp. 11786-11791
    • Yang, S.-D.1
  • 13
    • 0028176874 scopus 로고
    • A/Glycogen synthase kinase 3 predominantly phosphorylates the in vivo site Thr 97-Pro in brain myelin basic protein: Evidence for Thr-Pro and Ser-Arg-X-X-Ser as consensus sequence motifs
    • A/Glycogen synthase kinase 3 predominantly phosphorylates the in vivo site Thr 97-Pro in brain myelin basic protein: evidence for Thr-Pro and Ser-Arg-X-X-Ser as consensus sequence motifs. J. Neurochem. 62:1596-1603.
    • (1994) J. Neurochem. , vol.62 , pp. 1596-1603
    • Yu, J.-S.1    Yang, S.-D.2
  • 14
    • 0025258896 scopus 로고
    • Identification by Mass Spectrometry of Threonine 97 in Bovine Myelin Basic Protein as a specific phosphorylation site for Mitogen-activated Protein Kinase
    • Erickson, A. K., Payne, D. M., Martino, P. A., Rossomando, A. J., Shabanowitz, J., Weber, M. J., Hunt, D. F., and Sturgill, T. W. 1990. Identification by Mass Spectrometry of Threonine 97 in Bovine Myelin Basic Protein as a specific phosphorylation site for Mitogen-activated Protein Kinase. J. Biol. Chem. 265:19728-19735.
    • (1990) J. Biol. Chem. , vol.265 , pp. 19728-19735
    • Erickson, A.K.1    Payne, D.M.2    Martino, P.A.3    Rossomando, A.J.4    Shabanowitz, J.5    Weber, M.J.6    Hunt, D.F.7    Sturgill, T.W.8
  • 16
    • 0020673319 scopus 로고
    • Identification of multiple in vivo phosphorylation sites in rabbit myelin basic protein
    • Martenson, R. E., Law, M., and Deibler, G. E. 1983. Identification of multiple in vivo phosphorylation sites in rabbit myelin basic protein. J. Biol. Chem. 258:930-937.
    • (1983) J. Biol. Chem. , vol.258 , pp. 930-937
    • Martenson, R.E.1    Law, M.2    Deibler, G.E.3
  • 17
    • 0016801629 scopus 로고
    • The contribution of phosphorylation and loss of COOH-terminal arginine to the microheterogeneity of myelin basic protein
    • Deibler, G. E., Martenson, R. E., Kramer, A. J., Kies, M. W., and Miyamoto, E. 1975. The contribution of phosphorylation and loss of COOH-terminal arginine to the microheterogeneity of myelin basic protein. J. Biol. Chem. 250:7931-7938.
    • (1975) J. Biol. Chem. , vol.250 , pp. 7931-7938
    • Deibler, G.E.1    Martenson, R.E.2    Kramer, A.J.3    Kies, M.W.4    Miyamoto, E.5
  • 18
    • 0025366324 scopus 로고
    • Role of phosphorylation in conformational adaptability of bovine myelin basic protein
    • Deibler, G. E., Stome, A. L., and Kies, M. W. 1990. Role of phosphorylation in conformational adaptability of bovine myelin basic protein. Proteins 7:32-40.
    • (1990) Proteins , vol.7 , pp. 32-40
    • Deibler, G.E.1    Stome, A.L.2    Kies, M.W.3
  • 19
    • 0021251977 scopus 로고
    • Predicted folding of β-structure in myelin basic protein
    • Stoner, G. L. 1984. Predicted folding of β-structure in myelin basic protein. J. Neurochem. 43:433-447.
    • (1984) J. Neurochem. , vol.43 , pp. 433-447
    • Stoner, G.L.1
  • 20
    • 0020805751 scopus 로고
    • Phosphate groups modifying myelin basic proteins are metabolically labile; methyl groups are stable
    • Des Jardins, K. C., and Morell, P. 1983. Phosphate groups modifying myelin basic proteins are metabolically labile; methyl groups are stable. J. Cell. Biol. 97:438-446.
    • (1983) J. Cell. Biol. , vol.97 , pp. 438-446
    • Des Jardins, K.C.1    Morell, P.2
  • 22
    • 0022997313 scopus 로고
    • In vivo phosphorylation of myelin basic proteins: Single and double isotope incorporation in developmentally related myelin fractions
    • Ulmer, J. B., and Braun, P. E. 1986. In vivo phosphorylation of myelin basic proteins: single and double isotope incorporation in developmentally related myelin fractions. Dev. Biol. 117:502-510.
    • (1986) Dev. Biol. , vol.117 , pp. 502-510
    • Ulmer, J.B.1    Braun, P.E.2
  • 23
    • 0020335177 scopus 로고
    • 32P]orthophosphate into myelin basic protein of developing rabbit brain: Its location in components 3 and 5 and in a new protein tentatively identified as basic component 7
    • 32P]orthophosphate into myelin basic protein of developing rabbit brain: Its location in components 3 and 5 and in a new protein tentatively identified as basic component 7. J. Neurochem. 39:1755-1758.
    • (1982) J. Neurochem. , vol.39 , pp. 1755-1758
    • Agrawal, D.1    Martenson, R.E.2    Agrawal, H.C.3
  • 24
    • 0023753477 scopus 로고
    • Endogenous phosphorylation of basic protein in myelin of varying degrees of compaction
    • Schulz, P., Cruz, T. F., and Moscarello, M. A. 1988. Endogenous phosphorylation of basic protein in myelin of varying degrees of compaction. Biochemistry 27:7793-7799.
    • (1988) Biochemistry , vol.27 , pp. 7793-7799
    • Schulz, P.1    Cruz, T.F.2    Moscarello, M.A.3
  • 25
    • 0017691678 scopus 로고
    • Myelin basic protein phosphatase activity in rat brain
    • McNamara, J. O., and Appel, S. H. 1977. Myelin basic protein phosphatase activity in rat brain. J. Neurochem. 29:27-35.
    • (1977) J. Neurochem. , vol.29 , pp. 27-35
    • McNamara, J.O.1    Appel, S.H.2
  • 26
    • 0023147393 scopus 로고
    • Endogenous basic protein phosphatases in the brain myelin
    • Yang, S. D., Liu, J.-S., Fong, Y.-L., Yu, J.-S., and Tzen, T.-C. 1987. Endogenous basic protein phosphatases in the brain myelin. J. Neurochem. 48:160-166.
    • (1987) J. Neurochem. , vol.48 , pp. 160-166
    • Yang, S.D.1    Liu, J.-S.2    Fong, Y.-L.3    Yu, J.-S.4    Tzen, T.-C.5
  • 27
    • 0015609956 scopus 로고
    • Protein composition of myelin of the peripheral nervous system
    • Greenfield, S., Brostoff, S., Eylar, E. H., and Morell, P. 1973. Protein composition of myelin of the peripheral nervous system. J. Neurochem. 20:1207-1216.
    • (1973) J. Neurochem. , vol.20 , pp. 1207-1216
    • Greenfield, S.1    Brostoff, S.2    Eylar, E.H.3    Morell, P.4
  • 28
    • 0023967387 scopus 로고
    • Isolation and analysis of the gene encoding peripheral myelin protein zero
    • Lemke, G., Lamar, E., and Patterson, J. 1988. Isolation and analysis of the gene encoding peripheral myelin protein zero. Neuron 1:73-83.
    • (1988) Neuron , vol.1 , pp. 73-83
    • Lemke, G.1    Lamar, E.2    Patterson, J.3
  • 32
    • 0017139856 scopus 로고
    • Protein kinases associated with peripheral nerve myelin. I. Phosphorylation of endogenous myelin protein and exogenous substrates
    • Singh, H., and Spritz, N. 1976. Protein kinases associated with peripheral nerve myelin. I. Phosphorylation of endogenous myelin protein and exogenous substrates. Biochim. Biophys. Acta 448: 325-337.
    • (1976) Biochim. Biophys. Acta , vol.448 , pp. 325-337
    • Singh, H.1    Spritz, N.2
  • 33
    • 0018842160 scopus 로고
    • Phosphorylation and fucosylation of myelin proteins in vitro by sciatic nerve from developing rats
    • Wiggins, R. C., and Morell, P. 1980. Phosphorylation and fucosylation of myelin proteins in vitro by sciatic nerve from developing rats. J. Neurochem. 34:627-634.
    • (1980) J. Neurochem. , vol.34 , pp. 627-634
    • Wiggins, R.C.1    Morell, P.2
  • 36
    • 0024336792 scopus 로고
    • 0: Evidence for the presence of protein kinase C in purified PNS myelin
    • 0: Evidence for the presence of protein kinase C in purified PNS myelin. Neurochem. Res. 14:409-413.
    • (1989) Neurochem. Res. , vol.14 , pp. 409-413
    • Agrawal, H.C.1    Agrawal, D.2
  • 37
    • 0028168460 scopus 로고
    • 0 phosphorylation in nerves from normal and diabetic rats: Role of protein kinase C and turnover of phosphate roups
    • 0 phosphorylation in nerves from normal and diabetic rats: Role of protein kinase C and turnover of phosphate roups. Neurochem. Res. 19: 1023-1031.
    • (1994) Neurochem. Res. , vol.19 , pp. 1023-1031
    • Rowe-Rendleman, C.L.1    Eichberg, J.2
  • 38
    • 0028178093 scopus 로고
    • a, bI, bII, d and e protein kinase C isoforms and compound activity in the sciatic nerve of normal and diabetic rats
    • Borghini, I., Ania-Lahuerta, A., Regazzi, R., Ferrari, G., Gjnovci, A., Wollheim, C. B., and Pralong, W.-F. 1994. a, bI, bII, d and e protein kinase C isoforms and compound activity in the sciatic nerve of normal and diabetic rats. J. Neurochem. 61:686-696.
    • (1994) J. Neurochem. , vol.61 , pp. 686-696
    • Borghini, I.1    Ania-Lahuerta, A.2    Regazzi, R.3    Ferrari, G.4    Gjnovci, A.5    Wollheim, C.B.6    Pralong, W.-F.7
  • 40
    • 0023617436 scopus 로고
    • Altered protein phosphorylation in sciatic nerve from rats with streptozotocin-induced diabetes
    • Schrama, L. H., Berti-Mattera, L. N., and Eichberg, J. 1987. Altered protein phosphorylation in sciatic nerve from rats with streptozotocin-induced diabetes. Diabetes 36:1254-1260.
    • (1987) Diabetes , vol.36 , pp. 1254-1260
    • Schrama, L.H.1    Berti-Mattera, L.N.2    Eichberg, J.3
  • 42
    • 0028980525 scopus 로고
    • Myelin P0 glycoprotein: Identification of the site phosphorylated in vitro and in vivo by endogenous protein kinases
    • Hilmi, S., Fournier, M., Valeins, H., Gandar, J. C., and Bonnet, J. 1995. Myelin P0 glycoprotein: Identification of the site phosphorylated in vitro and in vivo by endogenous protein kinases. J. Neurochem. 64:902-907.
    • (1995) J. Neurochem. , vol.64 , pp. 902-907
    • Hilmi, S.1    Fournier, M.2    Valeins, H.3    Gandar, J.C.4    Bonnet, J.5
  • 43
    • 0028244197 scopus 로고
    • 0 interacts with negatively charged phospholipid bilayers
    • 0 interacts with negatively charged phospholipid bilayers. J. Biol. Chem. 269:10764-10770.
    • (1994) J. Biol. Chem. , vol.269 , pp. 10764-10770
    • Ding, Y.G.1    Brunden, K.R.2
  • 44
    • 0029067403 scopus 로고
    • PTB domain binding to signaling proteins through a sequence motif containing phosphotyrosine
    • Kavanaugh, W. M., Turck, C. W., and Williams, L. T. 1995. PTB domain binding to signaling proteins through a sequence motif containing phosphotyrosine. Science 268, 1177-1179.
    • (1995) Science , vol.268 , pp. 1177-1179
    • Kavanaugh, W.M.1    Turck, C.W.2    Williams, L.T.3
  • 45
    • 0029094991 scopus 로고
    • Specificity of the PTB domain of She for âturn-forming pentapeptide motifs amino terminal to phosphotyrosine
    • Trubi, T., Choi, W. E., Wolf, G., Ottinger, E., Chen, Y., Weiss, M., and Shoelson, S. 1995. Specificity of the PTB domain of She for âturn-forming pentapeptide motifs amino terminal to phosphotyrosine. J. Biol. Chem. 270:18205-18208.
    • (1995) J. Biol. Chem. , vol.270 , pp. 18205-18208
    • Trubi, T.1    Choi, W.E.2    Wolf, G.3    Ottinger, E.4    Chen, Y.5    Weiss, M.6    Shoelson, S.7
  • 46
    • 0025651203 scopus 로고
    • Myelin-associated glycoprotein: Location and potential functions
    • Duncan, I. D., Skoff, R. P. and Colman, D. (eds) Myelination and Dysmyelination
    • Trapp, B. D. 1990. Myelin-associated glycoprotein: Location and potential functions, in Duncan, I. D., Skoff, R. P. and Colman, D. (eds) Myelination and Dysmyelination. Ann. NY Acad. Sci. 605: 29-43.
    • (1990) Ann. NY Acad. Sci. , vol.605 , pp. 29-43
    • Trapp, B.D.1
  • 47
    • 0022186875 scopus 로고
    • Developmental expression of the myelin-associated glycoprotein in the peripheral nervous system is different from that in the central nervous system
    • Frail, D. E., Webster, H. D., and Braun, P. E. 1985. Developmental expression of the myelin-associated glycoprotein in the peripheral nervous system is different from that in the central nervous system. J. Neurochem. 45:1308-1310.
    • (1985) J. Neurochem. , vol.45 , pp. 1308-1310
    • Frail, D.E.1    Webster, H.D.2    Braun, P.E.3
  • 48
    • 0026090057 scopus 로고
    • Expression of the myelin-associated glycoprotein in cultures of immortalized Schwann cells
    • Goda, S., Hammer, J., Kobiler, D., and Quarles, R. H. 1991. Expression of the myelin-associated glycoprotein in cultures of immortalized Schwann cells. J. Neurochem. 56:1354-1361.
    • (1991) J. Neurochem. , vol.56 , pp. 1354-1361
    • Goda, S.1    Hammer, J.2    Kobiler, D.3    Quarles, R.H.4
  • 49
    • 0020060038 scopus 로고
    • Presence of the myelin-associated glycoprotein correlates with alterations in the periodicity of peripheral myelin
    • Trapp, B. D., and Quarles, R. H. 1982. Presence of the myelin-associated glycoprotein correlates with alterations in the periodicity of peripheral myelin. J. Cell. Biol. 92:877-882.
    • (1982) J. Cell. Biol. , vol.92 , pp. 877-882
    • Trapp, B.D.1    Quarles, R.H.2
  • 50
    • 0023917794 scopus 로고
    • Myelin-associated glycoprotein, a cell adhesion molecule of oligodendrocytes is phosphorylated in brain
    • Edwards, A. M., Arquint, M., Braun, P. E., Roder, J. C., Dunn, R. J., Pawson, T., and Bell, J. C. 1988. Myelin-associated glycoprotein, a cell adhesion molecule of oligodendrocytes is phosphorylated in brain. Mol. Cell. Biol. 8:2655-2658.
    • (1988) Mol. Cell. Biol. , vol.8 , pp. 2655-2658
    • Edwards, A.M.1    Arquint, M.2    Braun, P.E.3    Roder, J.C.4    Dunn, R.J.5    Pawson, T.6    Bell, J.C.7
  • 51
    • 0024502690 scopus 로고
    • Phosphorylation of myelin-associated glycoprotein in vivo and vitro occurs only in the cytoplasmic domain of large isoform
    • Edwards, A. M., Braun, P. E., and Bell, J. C. 1989. Phosphorylation of myelin-associated glycoprotein in vivo and vitro occurs only in the cytoplasmic domain of large isoform. J. Neurochem. 52:317-320.
    • (1989) J. Neurochem. , vol.52 , pp. 317-320
    • Edwards, A.M.1    Braun, P.E.2    Bell, J.C.3
  • 52
    • 0027489195 scopus 로고
    • Myelin-associated glycoprotein is phosphorylated by protein kinase C
    • Kirchhoff, F., Hofer, H. W., and Schachner, M. 1993. Myelin-associated glycoprotein is phosphorylated by protein kinase C. J. Neurosci. Res. 36:368-381.
    • (1993) J. Neurosci. Res. , vol.36 , pp. 368-381
    • Kirchhoff, F.1    Hofer, H.W.2    Schachner, M.3
  • 53
    • 0025087973 scopus 로고
    • Differential phosphorylation of myelin-associated glycoprotein isoforms in cell culture
    • Afar, D. E. H., Salzer, J. L., Roder, J., Braun, P. E., and Bell, J. C. 1990. Differential phosphorylation of myelin-associated glycoprotein isoforms in cell culture. J. Neurochem. 55:1418-1426.
    • (1990) J. Neurochem. , vol.55 , pp. 1418-1426
    • Afar, D.E.H.1    Salzer, J.L.2    Roder, J.3    Braun, P.E.4    Bell, J.C.5
  • 54
    • 0026320345 scopus 로고
    • Phosphorylation of myelin-associated glycoprotein in cultured oligodendrocytes
    • Bambrick, L. L., and Braun, P. E. 1991. Phosphorylation of myelin-associated glycoprotein in cultured oligodendrocytes. Dev. Neurosci. 13:412-416.
    • (1991) Dev. Neurosci. , vol.13 , pp. 412-416
    • Bambrick, L.L.1    Braun, P.E.2
  • 55
    • 0025313692 scopus 로고
    • The myelin-associated glycoprotein is phosphorylated in the peripheral nervous system
    • Agrawal, H. C., Noronha, A. B., Agrawal, D., and Quarles, R. H. 1990. The myelin-associated glycoprotein is phosphorylated in the peripheral nervous system. Biochem. Biophys. Res. Comm. 169: 953-958.
    • (1990) Biochem. Biophys. Res. Comm. , vol.169 , pp. 953-958
    • Agrawal, H.C.1    Noronha, A.B.2    Agrawal, D.3    Quarles, R.H.4
  • 57
    • 0023198136 scopus 로고
    • The amino acid sequence of the myelin-associated glycoproteins; homology to the immunoglobulin superfamily
    • Salzer, J. L., Holmes, P. W., and Colman, D. R. 1987. The amino acid sequence of the myelin-associated glycoproteins; homology to the immunoglobulin superfamily. J. Cell Biol. 104:957-965.
    • (1987) J. Cell Biol. , vol.104 , pp. 957-965
    • Salzer, J.L.1    Holmes, P.W.2    Colman, D.R.3
  • 58
    • 0027943833 scopus 로고
    • Identification of Tyr 620 as the major phosphorylation site of myelin-associated glycoprotein and its implication in interacting with signalling molecules
    • Jaramillo, M. L., Afar, D. E. H., Almazan, G., and Bell, J. C. 1994. Identification of Tyr 620 as the major phosphorylation site of myelin-associated glycoprotein and its implication in interacting with signalling molecules. J. Biol. Chem. 269:27240-27245.
    • (1994) J. Biol. Chem. , vol.269 , pp. 27240-27245
    • Jaramillo, M.L.1    Afar, D.E.H.2    Almazan, G.3    Bell, J.C.4
  • 60
    • 0027976632 scopus 로고
    • Initial events of myelination involve Fyn tyrosine kinase signalling
    • Umemori, H., Sato, S., Yagi, T., Alzawa, S., and Yamamoto, T. 1994. Initial events of myelination involve Fyn tyrosine kinase signalling. Nature 367:572-576.
    • (1994) Nature , vol.367 , pp. 572-576
    • Umemori, H.1    Sato, S.2    Yagi, T.3    Alzawa, S.4    Yamamoto, T.5
  • 62
    • 0023678987 scopus 로고
    • Cellular & 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 & subcellular distribution of 2′3′ Cyclic nucleotide 3′-phosphodiesterase and its mRNA in the rat central nervous system. J. Neurochem. 51:859-869.
    • (1988) J. Neurochem. , vol.51 , pp. 859-869
    • Trapp, B.D.1    Bernier, L.2    Andrews, S.B.3    Colman, D.R.4
  • 63
    • 0023925270 scopus 로고
    • Molecular structure, localization and possible functions of the myelin-associated enzyme 2′,3′-cyclic nucleotide 3′-phosphodiesterase
    • Vogel, U. S., and Thompson, R. J. 1988. Molecular structure, localization and possible functions of the myelin-associated enzyme 2′,3′-cyclic nucleotide 3′-phosphodiesterase. J. Neurochem. 50:1667-1677.
    • (1988) J. Neurochem. , vol.50 , pp. 1667-1677
    • Vogel, U.S.1    Thompson, R.J.2
  • 64
    • 0024600269 scopus 로고
    • 2′3′ Cyclic nucleotide 3′-phosphodiesterase, an oligodendrocyte-Schwann cell and myelin-associated enzyme of the nervous system
    • Sprinkle, T. J. 1989. 2′3′ Cyclic nucleotide 3′-phosphodiesterase, an oligodendrocyte-Schwann cell and myelin-associated enzyme of the nervous system. Crit. Rev. Neurobiol. 4(3):235-301.
    • (1989) Crit. Rev. Neurobiol. , vol.4 , Issue.3 , pp. 235-301
    • Sprinkle, T.J.1
  • 65
    • 0021193675 scopus 로고
    • Endogenous cyclic AMP-stimulated phosphorylation of a Wolfgram protein component in rabbit central nervous system myelin
    • Bradbury, J. M., Campbell, R. S., and Thompson, R. J. 1984. Endogenous cyclic AMP-stimulated phosphorylation of a Wolfgram protein component in rabbit central nervous system myelin. Biochem. J. 221:351-359.
    • (1984) Biochem. J. , vol.221 , pp. 351-359
    • Bradbury, J.M.1    Campbell, R.S.2    Thompson, R.J.3
  • 66
    • 0021225341 scopus 로고
    • Photoaffinity labeling of central nervous system myelin: Evidence for an endogenous cyclic AMP-dependent kinase phosphorylating the larger subunit of 2′3′-cyclic nucleotide 3′-phosphodiesterase
    • Bradbury, J. M., and Thompson, R. J. 1984. Photoaffinity labeling of central nervous system myelin: Evidence for an endogenous cyclic AMP-dependent kinase phosphorylating the larger subunit of 2′3′-cyclic nucleotide 3′-phosphodiesterase. Biochem. J. 221: 361-368.
    • (1984) Biochem. J. , vol.221 , pp. 361-368
    • Bradbury, J.M.1    Thompson, R.J.2
  • 67
    • 0026675064 scopus 로고
    • 2′,3′-cyclic nucleotide-3′-phosphohydrolase and signal transduction in central nervous system myelin
    • Thompson, R. J. 1992. 2′,3′-cyclic nucleotide-3′-phosphohydrolase and signal transduction in central nervous system myelin. Biochem. Soc. Transact. 20:621-626.
    • (1992) Biochem. Soc. Transact. , vol.20 , pp. 621-626
    • Thompson, R.J.1
  • 68
    • 0028227985 scopus 로고
    • In vivo phosphorylation of 2′,3′-cyclic nucleotide 3′-phosphohydrolase (CNP): CNP in brain myelin is phosphorylated by forskolin and phorbol ester-sensitive protein kinases
    • Agrawal, H. C., Sprinkle, T. J., and Agrawal, D. 1994. In vivo phosphorylation of 2′,3′-cyclic nucleotide 3′-phosphohydrolase (CNP): CNP in brain myelin is phosphorylated by forskolin and phorbol ester-sensitive protein kinases. Neurochem. Res. 19:721-728.
    • (1994) Neurochem. Res. , vol.19 , pp. 721-728
    • Agrawal, H.C.1    Sprinkle, T.J.2    Agrawal, D.3
  • 69
    • 0025127571 scopus 로고
    • 2′, 3′ cyclic nucleotide-3′-phosphodiesterase in peripheral nerve myelin is phosphorylated by a phorbol ester-sensitive protein kinase
    • Agrawal, H. C., Sprinkle, T. J., and Agrawal, D. 1990. 2′, 3′ cyclic nucleotide-3′-phosphodiesterase in peripheral nerve myelin is phosphorylated by a phorbol ester-sensitive protein kinase. Biochem. Biophys. Res. Comm. 170:817-823.
    • (1990) Biochem. Biophys. Res. Comm. , vol.170 , pp. 817-823
    • Agrawal, H.C.1    Sprinkle, T.J.2    Agrawal, D.3
  • 70
    • 0025696732 scopus 로고
    • 2′,3′-cyclic nucleotide-3′-phosphodiesterase has characteristics of cytoskeletal proteins: A hypothesis for its function
    • Duncan, I. D., Skoff, R. P. and Colman, D. (eds) Myelination and Dysmyelination, New York, NY
    • Braun, P. E., Bambrick, L. L., Edwards, A. M., and Bernier, L. 1990. 2′,3′-cyclic nucleotide-3′-phosphodiesterase has characteristics of cytoskeletal proteins: A hypothesis for its function, in Duncan, I. D., Skoff, R. P. and Colman, D. (eds) Myelination and Dysmyelination, Ann. New York Acad. Sci., New York, NY, pp. 55-65.
    • (1990) Ann. New York Acad. Sci. , pp. 55-65
    • Braun, P.E.1    Bambrick, L.L.2    Edwards, A.M.3    Bernier, L.4
  • 71
    • 0024535415 scopus 로고
    • Relationship of ATP turnover, polyphosphoinositide metabolism and protein phosphorylation in sciatic nerve and derived myelin subfractions from normal and streptozotocin diabetic rats
    • Lowery, J. M., Berti-Mattera, L. N., Zhu, X., Peterson, R. G., and Eichberg, J. 1989. Relationship of ATP turnover, polyphosphoinositide metabolism and protein phosphorylation in sciatic nerve and derived myelin subfractions from normal and streptozotocin diabetic rats. J. Neurochem. 52:921-932.
    • (1989) J. Neurochem. , vol.52 , pp. 921-932
    • Lowery, J.M.1    Berti-Mattera, L.N.2    Zhu, X.3    Peterson, R.G.4    Eichberg, J.5
  • 72
    • 0024395584 scopus 로고
    • Modulated adhesion - A proposal for the role of myelin-associated glycoprotein in myelin wrapping
    • Attia, J., Tropak, M., Johnson, P. W., Newerly-Abranow, W., Pawson, T., Roder, J. C., and Dunn, R. J. 1989. Modulated adhesion - a proposal for the role of myelin-associated glycoprotein in myelin wrapping. Clin Chem. 35:717-720.
    • (1989) Clin Chem. , vol.35 , pp. 717-720
    • Attia, J.1    Tropak, M.2    Johnson, P.W.3    Newerly-Abranow, W.4    Pawson, T.5    Roder, J.C.6    Dunn, R.J.7
  • 73
    • 0023513808 scopus 로고
    • Muscarinic receptor binding and muscarinic receptor-mediated inhibition of adenylate cyclase in rat brain myelin
    • Larocca, J. N., Makman, M. H., Golly, F., and Ledeen, R. W. 1987. Muscarinic receptor binding and muscarinic receptor-mediated inhibition of adenylate cyclase in rat brain myelin. J. Neurosci. 7:3869-3876.
    • (1987) J. Neurosci. , vol.7 , pp. 3869-3876
    • Larocca, J.N.1    Makman, M.H.2    Golly, F.3    Ledeen, R.W.4
  • 74
    • 0023472745 scopus 로고
    • Stimulation of phosphoinositide hydrolysis in myelin by muscarinic agonists and potassium
    • Larocca, J. N., Cervone, A., and Ledeen, R. W. 1987. Stimulation of phosphoinositide hydrolysis in myelin by muscarinic agonists and potassium. Brain. Res. 436:357-362.
    • (1987) Brain. Res. , vol.436 , pp. 357-362
    • Larocca, J.N.1    Cervone, A.2    Ledeen, R.W.3
  • 75
    • 0024336705 scopus 로고
    • Guanine nucleotides stimulate hydrolysis of phosphatidylinositol-4.5-bisphosphate in human myelin membranes
    • Boulias, C., and Moscarello, M. A. 1989. Guanine nucleotides stimulate hydrolysis of phosphatidylinositol-4.5-bisphosphate in human myelin membranes. Biochem. Biophys. Res. Commun. 162:282-287.
    • (1989) Biochem. Biophys. Res. Commun. , vol.162 , pp. 282-287
    • Boulias, C.1    Moscarello, M.A.2
  • 76
    • 0025285449 scopus 로고
    • Identification of GTP-binding proteins in myelin and oligodendrogliocyte membranes
    • Braun, P. E., Horvath, E., Yong, V. W., and Bernier, L. 1990. Identification of GTP-binding proteins in myelin and oligodendrogliocyte membranes. J. Neurosci. Res. 26:16-23.
    • (1990) J. Neurosci. Res. , vol.26 , pp. 16-23
    • Braun, P.E.1    Horvath, E.2    Yong, V.W.3    Bernier, L.4
  • 77
    • 0025649006 scopus 로고
    • Phosphoinositide breakdown in isolated myelin is stimulated by GTP analogs
    • Golly, F., Larocca, J. N., and Ledeen, R. W. 1990. Phosphoinositide breakdown in isolated myelin is stimulated by GTP analogs. J. Neurosci. Res. 27:342-348.
    • (1990) J. Neurosci. Res. , vol.27 , pp. 342-348
    • Golly, F.1    Larocca, J.N.2    Ledeen, R.W.3
  • 78
    • 0026075048 scopus 로고
    • Detection of G proteins in purified bovine brain myelin
    • Larocca, J. N., Golly, F. and Ledeen, R. W. 1991. Detection of G proteins in purified bovine brain myelin. J. Neurochem. 57:30-38.
    • (1991) J. Neurochem. , vol.57 , pp. 30-38
    • Larocca, J.N.1    Golly, F.2    Ledeen, R.W.3
  • 79
    • 0026629915 scopus 로고
    • Identification of G protein subtypes in peripheral nerve and cultured Schwann cells
    • Berti-Mattera, L. N., Goraya, T., Mattera, R., and Douglas, J. G. 1992. Identification of G protein subtypes in peripheral nerve and cultured Schwann cells. J. Neurochem. 59:1729-1735.
    • (1992) J. Neurochem. , vol.59 , pp. 1729-1735
    • Berti-Mattera, L.N.1    Goraya, T.2    Mattera, R.3    Douglas, J.G.4
  • 80
    • 0028055268 scopus 로고
    • Guanosine-5′-(3-O-thio)trisphosphate-mediated stimulation of phosphoinositidase C in solubilized rat peripheral nerve myelin and its alteration in streptozotocin-induced diabetes
    • Mathew, J., and Eichberg, J. 1994. Guanosine-5′-(3-O-thio)trisphosphate-mediated stimulation of phosphoinositidase C in solubilized rat peripheral nerve myelin and its alteration in streptozotocin-induced diabetes. J. Neurosci. Res. 37:83-91.
    • (1994) J. Neurosci. Res. , vol.37 , pp. 83-91
    • Mathew, J.1    Eichberg, J.2
  • 81
    • 0027240410 scopus 로고
    • Effects of hypoxia on oligodendrocyte signal transduction
    • Qi, Y., and Dawson, G. 1993. Effects of hypoxia on oligodendrocyte signal transduction. J. Neurochem. 61:1097-1104.
    • (1993) J. Neurochem. , vol.61 , pp. 1097-1104
    • Qi, Y.1    Dawson, G.2
  • 82
    • 0028353055 scopus 로고
    • Myelin membrane biogenesis by oligodendrocytes: Developmental regulation of low molecular weight GTP-binding proteins
    • Huber, L. A., Madison, D. L., Simons, K., and Pfeiffer, S. E. 1994. Myelin membrane biogenesis by oligodendrocytes: Developmental regulation of low molecular weight GTP-binding proteins. FEBS Letters 347:273-278.
    • (1994) FEBS Letters , vol.347 , pp. 273-278
    • Huber, L.A.1    Madison, D.L.2    Simons, K.3    Pfeiffer, S.E.4
  • 83
    • 34447112701 scopus 로고
    • Demonstration of members of the rho family of low-molecular weight GTPases in central nervous system myelin
    • Price, S. C., and Thompson, R. J. 1995. Demonstration of members of the rho family of low-molecular weight GTPases in central nervous system myelin. J. Neurochem. 65 (Suppl.): S142D.
    • (1995) J. Neurochem. , vol.65 , Issue.SUPPL.
    • Price, S.C.1    Thompson, R.J.2
  • 84
    • 0021960060 scopus 로고
    • Simple and rapid identification of phosphorylated peptides from bovine brain myelin basic protein by reversed phase high-performance liquid chromatography
    • Shoji, S., Ohnishi, J., Funakoshi, T., and Kubota, Y. 1985. Simple and rapid identification of phosphorylated peptides from bovine brain myelin basic protein by reversed phase high-performance liquid chromatography. J. Chromatography 319:359-366.
    • (1985) J. Chromatography , vol.319 , pp. 359-366
    • Shoji, S.1    Ohnishi, J.2    Funakoshi, T.3    Kubota, Y.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.