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Volumn 18, Issue 11, 2011, Pages 1422-1431

Deciphering the molecular details for the binding of the prion protein to main ganglioside GM1 of neuronal membranes

Author keywords

[No Author keywords available]

Indexed keywords

GANGLIOSIDE GM1; RECOMBINANT PROTEIN;

EID: 82255186663     PISSN: 10745521     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.chembiol.2011.08.016     Document Type: Article
Times cited : (40)

References (35)
  • 2
    • 33846419488 scopus 로고    scopus 로고
    • Lipid raft microdomains and neurotransmitter signalling
    • DOI 10.1038/nrn2059, PII NRN2059
    • J.A. Allen, R.A. Halverson-Tamboli, and M.M. Rasenick Lipid raft microdomains and neurotransmitter signalling Nat. Rev. Neurosci. 8 2007 128 140 (Pubitemid 46146951)
    • (2007) Nature Reviews Neuroscience , vol.8 , Issue.2 , pp. 128-140
    • Allen, J.A.1    Halverson-Tamboli, R.A.2    Rasenick, M.M.3
  • 5
    • 12544257523 scopus 로고    scopus 로고
    • In vitro conversion of full-length mammalian prion protein produces amyloid form with physical properties of PrP(Sc)
    • O.V. Bocharova, L. Breydo, A.S. Parfenov, V.V. Salnikov, and I.V. Baskakov In vitro conversion of full-length mammalian prion protein produces amyloid form with physical properties of PrP(Sc) J. Mol. Biol. 346 2005 645 659
    • (2005) J. Mol. Biol. , vol.346 , pp. 645-659
    • Bocharova, O.V.1    Breydo, L.2    Parfenov, A.S.3    Salnikov, V.V.4    Baskakov, I.V.5
  • 6
    • 0026775909 scopus 로고
    • Evidence for synthesis of scrapie prion proteins in the endocytic pathway
    • D.R. Borchelt, A. Taraboulos, and S.B. Prusiner Evidence for synthesis of scrapie prion proteins in the endocytic pathway J. Biol. Chem. 267 1992 16188 16199
    • (1992) J. Biol. Chem. , vol.267 , pp. 16188-16199
    • Borchelt, D.R.1    Taraboulos, A.2    Prusiner, S.B.3
  • 7
    • 0025991466 scopus 로고
    • The scrapie-associated form of PrP is made from a cell surface precursor that is both protease- and phospholipase-sensitive
    • B. Caughey, and G.J. Raymond The scrapie-associated form of PrP is made from a cell surface precursor that is both protease- and phospholipase-sensitive J. Biol. Chem. 266 1991 18217 18223 (Pubitemid 21908068)
    • (1991) Journal of Biological Chemistry , vol.266 , Issue.27 , pp. 18217-18223
    • Caughey, B.1    Raymond, G.J.2
  • 8
    • 67650747654 scopus 로고    scopus 로고
    • Getting a grip on prions: Oligomers, amyloids, and pathological membrane interactions
    • B. Caughey, G.S. Baron, B. Chesebro, and M. Jeffrey Getting a grip on prions: oligomers, amyloids, and pathological membrane interactions Annu. Rev. Biochem. 78 2009 177 204
    • (2009) Annu. Rev. Biochem. , vol.78 , pp. 177-204
    • Caughey, B.1    Baron, G.S.2    Chesebro, B.3    Jeffrey, M.4
  • 9
    • 0025876226 scopus 로고
    • N-terminal truncation of the scrapie-associated form of PrP by lysosomal protease(s): Implications regarding the site of conversion of PrP to the protease-resistant state
    • B. Caughey, G.J. Raymond, D. Ernst, and R.E. Race N-terminal truncation of the scrapie-associated form of PrP by lysosomal protease(s): implications regarding the site of conversion of PrP to the protease-resistant state J. Virol. 65 1991 6597 6603
    • (1991) J. Virol. , vol.65 , pp. 6597-6603
    • Caughey, B.1    Raymond, G.J.2    Ernst, D.3    Race, R.E.4
  • 12
    • 0031880893 scopus 로고    scopus 로고
    • Promotion of neuronal survival by GM1 ganglioside. Phenomenology and mechanism of action
    • G. Ferrari, and L.A. Greene Promotion of neuronal survival by GM1 ganglioside. Phenomenology and mechanism of action Ann. N Y Acad. Sci. 845 1998 263 273
    • (1998) Ann. N y Acad. Sci. , vol.845 , pp. 263-273
    • Ferrari, G.1    Greene, L.A.2
  • 13
    • 0037465821 scopus 로고    scopus 로고
    • Structural changes of the prion protein in lipid membranes leading to aggregation and fibrillization
    • DOI 10.1021/bi026872q
    • J. Kazlauskaite, N. Sanghera, I. Sylvester, C. Vénien-Bryan, and T.J.T. Pinheiro Structural changes of the prion protein in lipid membranes leading to aggregation and fibrillization Biochemistry 42 2003 3295 3304 (Pubitemid 36348638)
    • (2003) Biochemistry , vol.42 , Issue.11 , pp. 3295-3304
    • Kazlauskaite, J.1    Sanghera, N.2    Sylvester, I.3    Venien-Bryan, C.4    Pinheiro, T.J.T.5
  • 14
    • 0017840237 scopus 로고
    • Ganglioside structures and distribution: Are they localized at the nerve ending?
    • R.W. Ledeen Ganglioside structures and distribution: are they localized at the nerve ending? J. Supramol. Struct. 8 1978 1 17 (Pubitemid 8328309)
    • (1978) Journal of Supramolecular and Cellular Biochemistry , vol.8 , Issue.1 , pp. 1-17
    • Ledeen, R.W.1
  • 15
    • 0031949027 scopus 로고    scopus 로고
    • The role of GM1 and other gangliosides in neuronal differentiation. Overview and new finding
    • R.W. Ledeen, G. Wu, Z.H. Lu, D. Kozireski-Chuback, and Y. Fang The role of GM1 and other gangliosides in neuronal differentiation. Overview and new finding Ann. N Y Acad. Sci. 845 1998 161 175
    • (1998) Ann. N y Acad. Sci. , vol.845 , pp. 161-175
    • Ledeen, R.W.1    Wu, G.2    Lu, Z.H.3    Kozireski-Chuback, D.4    Fang, Y.5
  • 17
    • 27144547245 scopus 로고    scopus 로고
    • Exogenous gangliosides, neuronal plasticity and repair, and the neurotrophins
    • DOI 10.1007/s00018-005-5188-y
    • I. Mocchetti Exogenous gangliosides, neuronal plasticity and repair, and the neurotrophins Cell. Mol. Life Sci. 62 2005 2283 2294 (Pubitemid 41500544)
    • (2005) Cellular and Molecular Life Sciences , vol.62 , Issue.19-20 , pp. 2283-2294
    • Mocchetti, I.1
  • 18
    • 0033601248 scopus 로고    scopus 로고
    • Membrane environment alters the conformational structure of the recombinant human prion protein
    • M. Morillas, W. Swietnicki, P. Gambetti, and W.K. Surewicz Membrane environment alters the conformational structure of the recombinant human prion protein J. Biol. Chem. 274 1999 36859 36865
    • (1999) J. Biol. Chem. , vol.274 , pp. 36859-36865
    • Morillas, M.1    Swietnicki, W.2    Gambetti, P.3    Surewicz, W.K.4
  • 20
    • 1642334714 scopus 로고    scopus 로고
    • M1/dipalmitoylphosphatidylcholine/dioleoylphosphatidylcholine
    • DOI 10.1016/j.colsurfb.2003.11.005, PII S0927776503002844
    • Y. Ohta, S. Yokoyama, H. Sakai, and M. Abe Membrane properties of binary and ternary systems of ganglioside GM1/dipalmitoylphosphatidylcholine/ dioleoylphosphatidylcholine Colloids Surf. B Biointerfaces 34 2004 147 153 (Pubitemid 38369346)
    • (2004) Colloids and Surfaces B: Biointerfaces , vol.34 , Issue.3 , pp. 147-153
    • Ohta, Y.1    Yokoyama, S.2    Sakai, H.3    Abe, M.4
  • 21
    • 0023049085 scopus 로고
    • 1H-NMR assignments of GM1-oligosaccharide in deuterated water at 500 MHz by two-dimensional spin-echo J-correlated spectroscopy
    • R.L. Ong, and R.K. Yu 1H-NMR assignments of GM1-oligosaccharide in deuterated water at 500 MHz by two-dimensional spin-echo J-correlated spectroscopy Arch. Biochem. Biophys. 245 1986 157 166
    • (1986) Arch. Biochem. Biophys. , vol.245 , pp. 157-166
    • Ong, R.L.1    Yu, R.K.2
  • 22
    • 33646550550 scopus 로고    scopus 로고
    • The role of rafts in the fibrillization and aggregation of prions
    • DOI 10.1016/j.chemphyslip.2006.02.022, PII S0009308406000259
    • T.J. Pinheiro The role of rafts in the fibrillization and aggregation of prions Chem. Phys. Lipids 141 2006 66 71 (Pubitemid 43728805)
    • (2006) Chemistry and Physics of Lipids , vol.141 , Issue.1-2 , pp. 66-71
    • Pinheiro, T.J.T.1
  • 24
    • 70149110670 scopus 로고    scopus 로고
    • The unfolding of the prion protein sheds light on the mechanisms of prion susceptibility and species barrier
    • P.J. Robinson, and T.J. Pinheiro The unfolding of the prion protein sheds light on the mechanisms of prion susceptibility and species barrier Biochemistry 48 2009 8551 8558
    • (2009) Biochemistry , vol.48 , pp. 8551-8558
    • Robinson, P.J.1    Pinheiro, T.J.2
  • 25
    • 79960904305 scopus 로고    scopus 로고
    • Common structural traits across pathogenic mutants of the human prion protein and their implications for familial prion diseases
    • G. Rossetti, X. Cong, R. Caliandro, G. Legname, and P. Carloni Common structural traits across pathogenic mutants of the human prion protein and their implications for familial prion diseases J. Mol. Biol. 411 2011 700 712
    • (2011) J. Mol. Biol. , vol.411 , pp. 700-712
    • Rossetti, G.1    Cong, X.2    Caliandro, R.3    Legname, G.4    Carloni, P.5
  • 26
    • 0036306046 scopus 로고    scopus 로고
    • Binding of prion protein to lipid membranes and implications for prion conversion
    • DOI 10.1006/jmbi.2001.5322
    • N. Sanghera, and T.J. Pinheiro Binding of prion protein to lipid membranes and implications for prion conversion J. Mol. Biol. 315 2002 1241 1256 (Pubitemid 34729301)
    • (2002) Journal of Molecular Biology , vol.315 , Issue.5 , pp. 1241-1256
    • Sanghera, N.1    Pinheiro, T.J.T.2
  • 27
    • 43649097136 scopus 로고    scopus 로고
    • Globular and pre-fibrillar prion aggregates are toxic to neuronal cells and perturb their electrophysiology
    • N. Sanghera, M. Wall, C. Vénien-Bryan, and T.J. Pinheiro Globular and pre-fibrillar prion aggregates are toxic to neuronal cells and perturb their electrophysiology Biochim. Biophys. Acta 1784 2008 873 881
    • (2008) Biochim. Biophys. Acta , vol.1784 , pp. 873-881
    • Sanghera, N.1    Wall, M.2    Vénien-Bryan, C.3    Pinheiro, T.J.4
  • 28
    • 0028151351 scopus 로고
    • Interactions between saturated acyl chains confer detergent resistance on lipids and glycosylphosphatidylinositol (GPI)-anchored proteins: GPI-anchored proteins in liposomes and cells show similar behavior
    • R. Schroeder, E. London, and D. Brown Interactions between saturated acyl chains confer detergent resistance on lipids and glycosylphosphatidylinositol (GPI)-anchored proteins: GPI-anchored proteins in liposomes and cells show similar behavior Proc. Natl. Acad. Sci. USA 91 1994 12130 12134
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 12130-12134
    • Schroeder, R.1    London, E.2    Brown, D.3
  • 29
    • 0023663071 scopus 로고
    • Scrapie prion protein contains a phosphatidylinositol glycolipid
    • N. Stahl, D.R. Borchelt, K. Hsiao, and S.B. Prusiner Scrapie prion protein contains a phosphatidylinositol glycolipid Cell 51 1987 229 240
    • (1987) Cell , vol.51 , pp. 229-240
    • Stahl, N.1    Borchelt, D.R.2    Hsiao, K.3    Prusiner, S.B.4
  • 30
    • 4444355320 scopus 로고    scopus 로고
    • M1-ganglioside-mediated activation of the unfolded protein response causes neuronal death in a neurodegenerative gangliosidosis
    • DOI 10.1016/j.molcel.2004.08.029, PII S1097276504005131
    • A. Tessitore, M. del P Martin, R. Sano, Y. Ma, L. Mann, A. Ingrassia, E.D. Laywell, D.A. Steindler, L.M. Hendershot, and A. d'Azzo GM1-ganglioside-mediated activation of the unfolded protein response causes neuronal death in a neurodegenerative gangliosidosis Mol. Cell 15 2004 753 766 (Pubitemid 39194905)
    • (2004) Molecular Cell , vol.15 , Issue.5 , pp. 753-766
    • Tessitore, A.1    Martin, M.D.P.2    Sano, R.3    Ma, Y.4    Mann, L.5    Ingrassia, A.6    Laywell, E.D.7    Steindler, D.A.8    Hendershot, L.M.9    D'Azzo, A.10
  • 31
    • 33744826819 scopus 로고    scopus 로고
    • MolDock: A new technique for high-accuracy molecular docking
    • DOI 10.1021/jm051197e
    • R. Thomsen, and M.H. Christensen MolDock: a new technique for high-accuracy molecular docking J. Med. Chem. 49 2006 3315 3321 (Pubitemid 43830529)
    • (2006) Journal of Medicinal Chemistry , vol.49 , Issue.11 , pp. 3315-3321
    • Thomsen, R.1    Christensen, M.H.2
  • 33
    • 77649213673 scopus 로고    scopus 로고
    • Generating a prion with bacterially expressed recombinant prion protein
    • F. Wang, X.H. Wang, C.G. Yuan, and J.Y. Ma Generating a prion with bacterially expressed recombinant prion protein Science 327 2010 1132 1135
    • (2010) Science , vol.327 , pp. 1132-1135
    • Wang, F.1    Wang, X.H.2    Yuan, C.G.3    Ma, J.Y.4
  • 35
    • 77649270452 scopus 로고    scopus 로고
    • NMR characterization of the interactions between lyso-GM1 aqueous micelles and amyloid beta
    • M. Yagi-Utsumi, T. Kameda, Y. Yamaguchi, and K. Kato NMR characterization of the interactions between lyso-GM1 aqueous micelles and amyloid beta FEBS Lett. 584 2010 831 836
    • (2010) FEBS Lett. , vol.584 , pp. 831-836
    • Yagi-Utsumi, M.1    Kameda, T.2    Yamaguchi, Y.3    Kato, K.4


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