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Volumn 99, Issue 9, 2010, Pages 3020-3028

Copper uptake induces self-assembly of 18.5 kDa myelin basic protein (MBP)

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EID: 78349250611     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1016/j.bpj.2010.08.022     Document Type: Article
Times cited : (20)

References (30)
  • 1
    • 0034065232 scopus 로고    scopus 로고
    • On the molecular architecture of myelinated fibers
    • Arroyo, E. J., and S. S. Scherer. 2000. On the molecular architecture of myelinated fibers. Histochem. Cell Biol. 113:1-18.
    • (2000) Histochem. Cell. Biol. , vol.113 , pp. 1-18
    • Arroyo, E.J.1    Scherer, S.S.2
  • 2
    • 0035066639 scopus 로고    scopus 로고
    • Biology of oligodendrocyte and myelin in the mammalian central nervous system
    • Baumann, N., and D. Pham-Dinh. 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
  • 3
    • 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
  • 4
    • 3042553626 scopus 로고    scopus 로고
    • Myelin basic proteindiverse conformational states of an intrinsically unstructured protein and its roles in myelin assembly and multiple sclerosis
    • Harauz, G., N. Ishiyama., C. Farès. 2004. Myelin basic proteindiverse 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    Farès, C.3
  • 5
    • 0022336444 scopus 로고
    • Alternative splicing accounts for the four forms of myelin basic protein
    • de Ferra, F., H. Engh., R. A. Lazzarini. 1985. Alternative splicing accounts for the four forms of myelin basic protein. Cell. 43:721-727.
    • (1985) Cell. , vol.43 , pp. 721-727
    • De Ferra, F.1    Engh, H.2    Lazzarini, R.A.3
  • 6
    • 0034650979 scopus 로고    scopus 로고
    • New insights on the biology of myelin basic protein gene: The neuralimmune connection
    • Givogri, M. I., E. R. Bongarzone, and A. T. Campagnoni. 2000. New insights on the biology of myelin basic protein gene: the neuralimmune connection. J. Neurosci. Res. 59:153-159.
    • (2000) J. Neurosci. Res. , vol.59 , pp. 153-159
    • Givogri, M.I.1    Bongarzone, E.R.2    Campagnoni, A.T.3
  • 7
    • 0025758988 scopus 로고
    • Regulation of myelin basic protein gene transcription in glial cells
    • Asipu, A., and G. E. Blair. 1991. Regulation of myelin basic protein gene transcription in glial cells. Biochem. Soc. Trans. 19:85S.
    • (1991) Biochem. Soc. Trans. , vol.19
    • Asipu, A.1    Blair, G.E.2
  • 8
    • 0036423128 scopus 로고    scopus 로고
    • Effects of the osmolyte trimethylamine-N-oxide on conformation, self-association, and twodimensional crystallization of myelin basic protein
    • Hill, C. M., I. R. Bates., G. Harauz. 2002. Effects of the osmolyte trimethylamine-N-oxide on conformation, self-association, and twodimensional crystallization of myelin basic protein. J. Struct. Biol. 139:13-26.
    • (2002) J. Struct. Biol. , vol.139 , pp. 13-26
    • Hill, C.M.1    Bates, I.R.2    Harauz, G.3
  • 9
    • 0037264876 scopus 로고    scopus 로고
    • Terminal deletion mutants of myelin basic protein: New insights into self-association and phospholipid interactions
    • Hill, C. M. D., J. D. Haines., G. Harauz. 2003. Terminal deletion mutants of myelin basic protein: new insights into self-association and phospholipid interactions. Micron. 34:25-37.
    • (2003) Micron , vol.34 , pp. 25-37
    • Hill, C.M.D.1    Haines, J.D.2    Harauz, G.3
  • 10
    • 0041384333 scopus 로고    scopus 로고
    • The N-terminal domain of p53 is natively unfolded
    • Dawson, R., L. Müller., J. Buchner. 2003. The N-terminal domain of p53 is natively unfolded. J. Mol. Biol. 332:1131-1141.
    • (2003) J. Mol. Biol. , vol.332 , pp. 1131-1141
    • Dawson, R.1    Müller, L.2    Buchner, J.3
  • 11
    • 0142234077 scopus 로고    scopus 로고
    • Multiple sclerosis: An important role for post-translational modifications of myelin basic protein in pathogenesis
    • Kim, J. K., F. G. Mastronardi., M. A. Moscarello. 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    Moscarello, M.A.3
  • 12
    • 0027941087 scopus 로고
    • Divalent metals of myelin and their differential binding by myelin basic protein of bovine central nervous system
    • Berlet, H. H., H. Bischoff, and F. Weinhardt. 1994. Divalent metals of myelin and their differential binding by myelin basic protein of bovine central nervous system. Neurosci. Lett. 179:75-78.
    • (1994) Neurosci. Lett. , vol.179 , pp. 75-78
    • Berlet, H.H.1    Bischoff, H.2    Weinhardt, F.3
  • 13
    • 0028316187 scopus 로고
    • Myelin basic protein interaction with zinc and phosphate: Fluorescence studies on the water-soluble form of the protein
    • Cavatorta, P., S. Giovanelli., E. Quagliariello. 1994. Myelin basic protein interaction with zinc and phosphate: fluorescence studies on the water-soluble form of the protein. Biophys. J. 66:1174-1179.
    • (1994) Biophys. J. , vol.66 , pp. 1174-1179
    • Cavatorta, P.1    Giovanelli, S.2    Quagliariello, E.3
  • 14
    • 0028788026 scopus 로고
    • Specificity of zinc binding to myelin basic protein
    • Riccio, P., S. Giovannelli., P. Cavatorta. 1995. Specificity of zinc binding to myelin basic protein. Neurochem. Res. 20:1107-1113.
    • (1995) Neurochem. Res. , vol.20 , pp. 1107-1113
    • Riccio, P.1    Giovannelli, S.2    Cavatorta, P.3
  • 15
    • 72949107606 scopus 로고    scopus 로고
    • Divalent cations induce a compaction of intrinsically disordered myelin basic protein
    • Baran, C., G. S. Smith., J. S. Lee. 2010. Divalent cations induce a compaction of intrinsically disordered myelin basic protein. Biochem. Biophys. Res. Commun. 391:224-229.
    • (2010) Biochem. Biophys. Res. Commun. , vol.391 , pp. 224-229
    • Baran, C.1    Smith, G.S.2    Lee, J.S.3
  • 16
    • 0030878113 scopus 로고    scopus 로고
    • Myelin basic protein is a zinc-binding protein in brain: Possible role in myelin compaction
    • Tsang, D., Y. S. Tsang., R. N. Wong. 1997. Myelin basic protein is a zinc-binding protein in brain: possible role in myelin compaction. Neurochem. Res. 22:811-819.
    • (1997) Neurochem. Res. , vol.22 , pp. 811-819
    • Tsang, D.1    Tsang, Y.S.2    Wong, R.N.3
  • 17
    • 0037050044 scopus 로고    scopus 로고
    • Thermodynamics of binding copper ion by myelin basic protein
    • Saboury, A. A., N. Sarri-Sarraf, and S. Saidian. 2002. Thermodynamics of binding copper ion by myelin basic protein. Thermochim. Acta. 381:147-151.
    • (2002) Thermochim. Acta , vol.381 , pp. 147-151
    • Saboury, A.A.1    Sarri-Sarraf, N.2    Saidian, S.3
  • 18
    • 77956916946 scopus 로고    scopus 로고
    • The interaction of zinc with membrane-associated 18.5 kDa myelin basic protein: An attenuated total reflectance-Fourier transform infrared spectroscopic study
    • Smith, G. S., L. Chen., G. Harauz. 2010. The interaction of zinc with membrane-associated 18.5 kDa myelin basic protein: an attenuated total reflectance-Fourier transform infrared spectroscopic study. Amino Acids. 39:739-750.
    • (2010) Amino Acids , vol.39 , pp. 739-750
    • Smith, G.S.1    Chen, L.2    Harauz, G.3
  • 19
    • 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 M. A. Moscarello. 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
  • 20
    • 49149093778 scopus 로고    scopus 로고
    • Quantification of the binding constant of copper (II) to the amyloid-β peptide
    • Hatcher, L. Q., L. Hong., J. D. Simon. 2008. Quantification of the binding constant of copper (II) to the amyloid-β peptide. J. Phys. Chem. B. 112:8160-8164.
    • (2008) J. Phys. Chem. B. , vol.112 , pp. 8160-8164
    • Hatcher, L.Q.1    Hong, L.2    Simon, J.D.3
  • 21
    • 0029866476 scopus 로고    scopus 로고
    • Two-dimensional pulsed EPR spectroscopy of the copper protein azurin
    • Kofman, V., O. Farver, I. Pecht, and D. Goldfarb. 1996. Two-dimensional pulsed EPR spectroscopy of the copper protein azurin. J. Am. Chem. Soc. 118:1201-1206.
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 1201-1206
    • Kofman, V.1    Farver, O.2    Pecht, I.3    Goldfarb, D.4
  • 22
    • 61749097242 scopus 로고    scopus 로고
    • Pleomorphic copper coordination by Alzheimer's disease amyloid-β peptide
    • Drew, S. C., C. J. Noble., K. J. Barnham. 2009. Pleomorphic copper coordination by Alzheimer's disease amyloid-β peptide. J. Am. Chem. Soc. 131:1195-1207.
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 1195-1207
    • Drew, S.C.1    Noble, C.J.2    Barnham, K.J.3
  • 24
    • 46349097539 scopus 로고    scopus 로고
    • PELDOR measurements on a nitroxide-labeled Cu (II) porphyrin: Orientation selection, spin-density distribution, and conformational flexibility
    • Bode, B. E., J. Plackmeyer., O. Schiemann. 2008. PELDOR measurements on a nitroxide-labeled Cu (II) porphyrin: orientation selection, spin-density distribution, and conformational flexibility. J. Phys. Chem. A. 112:5064-5073.
    • (2008) J. Phys. Chem. A , vol.112 , pp. 5064-5073
    • Bode, B.E.1    Plackmeyer, J.2    Schiemann, O.3
  • 25
    • 0033960382 scopus 로고    scopus 로고
    • Causes of iron and zinc deficiencies and their effects on brain
    • Sandstead, H. H. 2000. Causes of iron and zinc deficiencies and their effects on brain. J. Nutr. 130:347S-349S.
    • (2000) J. Nutr. , vol.130
    • Sandstead, H.H.1
  • 26
    • 59149098864 scopus 로고    scopus 로고
    • Copper and the structural biology of the prion protein
    • Viles, J. H., M. Klewpatinond, and R. C. Nadal. 2008. Copper and the structural biology of the prion protein. Biochem. Soc. Trans. 36:1288-1292.
    • (2008) Biochem. Soc. Trans. , vol.36 , pp. 1288-1292
    • Viles, J.H.1    Klewpatinond, M.2    Nadal, R.C.3
  • 27
    • 69949167074 scopus 로고    scopus 로고
    • Zn (II)-and Cu (II)-induced non-fibrillar aggregates of amyloid-β (1-42) peptide are transformed to amyloid fibrils, both spontaneously and under the influence of metal chelators
    • Tõugu, V., A. Karafin., P. Palumaa. 2009. Zn (II)-and Cu (II)-induced non-fibrillar aggregates of amyloid-β (1-42) peptide are transformed to amyloid fibrils, both spontaneously and under the influence of metal chelators. J. Neurochem. 110:1784-1795.
    • (2009) J. Neurochem. , vol.110 , pp. 1784-1795
    • Tõugu, V.1    Karafin, A.2    Palumaa, P.3
  • 28
    • 71449117143 scopus 로고    scopus 로고
    • The cuprizone animal model: New insights into an old story
    • Kipp, M., T. Clarner., C. Beyer. 2009. The cuprizone animal model: new insights into an old story. Acta Neuropathol. 118:723-736.
    • (2009) Acta Neuropathol. , vol.118 , pp. 723-736
    • Kipp, M.1    Clarner, T.2    Beyer, C.3
  • 29
    • 66149161888 scopus 로고    scopus 로고
    • Copper (II) binding to amyloid-β fibrils of Alzheimer's disease reveals a picomolar affinity: Stoichiometry and coordination geometry are independent of Aβ oligomeric form
    • Sarell, C. J., C. D. Syme., J. H. Viles. 2009. Copper (II) binding to amyloid-β fibrils of Alzheimer's disease reveals a picomolar affinity: stoichiometry and coordination geometry are independent of Aβ oligomeric form. Biochemistry. 48:4388-4402.
    • (2009) Biochemistry , vol.48 , pp. 4388-4402
    • Sarell, C.J.1    Syme, C.D.2    Viles, J.H.3
  • 30
    • 45849135972 scopus 로고    scopus 로고
    • Solution NMR and CD spectroscopy of an intrinsically disordered, peripheral membrane protein: Evaluation of aqueous and membrane-mimetic solvent conditions for studying the conformational adaptability of the 18.5 kDa isoform of myelin basic protein (MBP)
    • Libich, D. S., and G. Harauz. 2008. Solution NMR and CD spectroscopy of an intrinsically disordered, peripheral membrane protein: evaluation of aqueous and membrane-mimetic solvent conditions for studying the conformational adaptability of the 18.5 kDa isoform of myelin basic protein (MBP). Eur. Biophys. J. 37:1015-1029.
    • (2008) Eur. Biophys. J. , vol.37 , pp. 1015-1029
    • Libich, D.S.1    Harauz, G.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.