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Volumn 6, Issue 3, 2015, Pages 374-379

α-Synuclein insertion into supported lipid bilayers as seen by in situ X-ray reflectivity

Author keywords

Parkinsons disease; supported lipid bilayer; X ray reflectivity; Synuclein

Indexed keywords

ALPHA SYNUCLEIN; MUTANT PROTEIN; PROTEIN VARIANT; LIPID BILAYER;

EID: 84925082253     PISSN: None     EISSN: 19487193     Source Type: Journal    
DOI: 10.1021/cn5002683     Document Type: Article
Times cited : (8)

References (33)
  • 6
    • 80555155665 scopus 로고    scopus 로고
    • The role of a -synuclein in neurotransmission and synaptic plasticity
    • Cheng, F., Vivacqua, G., and Yu, S. (2011) The role of a -synuclein in neurotransmission and synaptic plasticity J. Chem. Neuroanat. 42, 242-248
    • (2011) J. Chem. Neuroanat. , vol.42 , pp. 242-248
    • Cheng, F.1    Vivacqua, G.2    Yu, S.3
  • 7
    • 0032540327 scopus 로고    scopus 로고
    • Stabilization of alpha-synuclein secondary structure upon binding to synthetic membranes
    • Davidson, W. S., Jonas, A., Clayton, D. F., and George, J. M. (1998) Stabilization of alpha-synuclein secondary structure upon binding to synthetic membranes J. Biol. Chem. 273, 9443-9449
    • (1998) J. Biol. Chem. , vol.273 , pp. 9443-9449
    • Davidson, W.S.1    Jonas, A.2    Clayton, D.F.3    George, J.M.4
  • 8
    • 77958449984 scopus 로고    scopus 로고
    • α-Synuclein: Membrane interactions and toxicity in Parkinsons disease
    • Auluck, P. K., Caraveo, G., and Lindquist, S. (2010) α-Synuclein: Membrane interactions and toxicity in Parkinsons disease Annu. Rev. Cell Dev. Biol. 26, 211-233
    • (2010) Annu. Rev. Cell Dev. Biol. , vol.26 , pp. 211-233
    • Auluck, P.K.1    Caraveo, G.2    Lindquist, S.3
  • 9
    • 78650763561 scopus 로고    scopus 로고
    • Membrane Permeabilization by Oligomeric α-Synuclein: In Search of the Mechanism
    • van Rooijen, B. D., Claessens, M. M. A. E., and Subramaniam, V. (2010) Membrane Permeabilization by Oligomeric α-Synuclein: In Search of the Mechanism PLoS One 5, e14292
    • (2010) PLoS One , vol.5 , pp. 14292
    • Van Rooijen, B.D.1    Claessens, M.M.A.E.2    Subramaniam, V.3
  • 11
    • 84875553835 scopus 로고    scopus 로고
    • On-surface aggregation of α-synuclein at nanomolar concentrations results in two distinct growth mechanisms
    • Rabe, M., Soragni, A., Reynolds, N. P., Verdes, D., Liverani, E., Riek, R., and Seeger, S. (2013) On-surface aggregation of α-synuclein at nanomolar concentrations results in two distinct growth mechanisms ACS Chem. Neurosci. 4, 408-417
    • (2013) ACS Chem. Neurosci. , vol.4 , pp. 408-417
    • Rabe, M.1    Soragni, A.2    Reynolds, N.P.3    Verdes, D.4    Liverani, E.5    Riek, R.6    Seeger, S.7
  • 12
    • 79952742454 scopus 로고    scopus 로고
    • In vivo demonstration that alpha-synuclein oligomers are toxic
    • Winner, B. 2011, In vivo demonstration that alpha-synuclein oligomers are toxic Proc. Natl. Acad. Sci. U. S. A. 108, 4194-4199
    • (2011) Proc. Natl. Acad. Sci. U. S. A. , vol.108 , pp. 4194-4199
    • Winner, B.1
  • 13
    • 84877011946 scopus 로고    scopus 로고
    • Using in situ X-ray reflectivity to study protein adsorption on hydrophilic and hydrophobic surfaces: Benefits and limitations
    • Richter, A. G. and Kuzmenko, I. (2013) Using in situ X-ray reflectivity to study protein adsorption on hydrophilic and hydrophobic surfaces: benefits and limitations Langmuir 29, 5167-5180
    • (2013) Langmuir , vol.29 , pp. 5167-5180
    • Richter, A.G.1    Kuzmenko, I.2
  • 15
    • 25844445954 scopus 로고    scopus 로고
    • A microfluidic setup for studies of solid-liquid interfaces using X-ray reflectivity and fluorescence microscopy
    • Reich, C., Hochrein, M., Krause, B., and Nickel, B. (2005) A microfluidic setup for studies of solid-liquid interfaces using X-ray reflectivity and fluorescence microscopy Rev. Sci. Instrum. 76, 095103
    • (2005) Rev. Sci. Instrum. , vol.76 , pp. 095103
    • Reich, C.1    Hochrein, M.2    Krause, B.3    Nickel, B.4
  • 16
    • 40949103430 scopus 로고    scopus 로고
    • In situ X-ray reflectivity studies on the formation of substrate-supported phospholipid bilayers and monolayers
    • Wang, S. T., Fukuto, M., and Yang, L. (2008) In situ X-ray reflectivity studies on the formation of substrate-supported phospholipid bilayers and monolayers Phys. Rev. E 77, 31909
    • (2008) Phys. Rev. e , vol.77 , pp. 31909
    • Wang, S.T.1    Fukuto, M.2    Yang, L.3
  • 17
    • 84894481810 scopus 로고    scopus 로고
    • The presence of an air-water interface affects formation and elongation of a -synuclein fibrils
    • Campioni, S., Carret, G., Jordens, S., Nicoud, L., Mezzenga, R., and Riek, J. (2014) The presence of an air-water interface affects formation and elongation of a -synuclein fibrils J. Am. Chem. Soc. 136, 2866-2875
    • (2014) J. Am. Chem. Soc. , vol.136 , pp. 2866-2875
    • Campioni, S.1    Carret, G.2    Jordens, S.3    Nicoud, L.4    Mezzenga, R.5    Riek, J.6
  • 18
    • 0242290843 scopus 로고    scopus 로고
    • Pathways of lipid vesicle deposition on solid surfaces: A combined QCM-D and AFM study
    • Richter, R., Mukhopadhyay, A., and Brisson, A. (2003) Pathways of lipid vesicle deposition on solid surfaces: a combined QCM-D and AFM study Biophys. J. 85, 3035-3047
    • (2003) Biophys. J. , vol.85 , pp. 3035-3047
    • Richter, R.1    Mukhopadhyay, A.2    Brisson, A.3
  • 21
    • 26144449160 scopus 로고
    • Surface studies of solids by total reflection of X-rays
    • Parratt, L. G. (1954) Surface studies of solids by total reflection of X-rays Phys. Rev. 95, 359-369
    • (1954) Phys. Rev. , vol.95 , pp. 359-369
    • Parratt, L.G.1
  • 22
    • 84925111969 scopus 로고    scopus 로고
    • The Center for X-ray Optics
    • The Center for X-ray Optics. http://www.cxro.lbl.gov/.
  • 24
    • 84863012541 scopus 로고    scopus 로고
    • Depth of a-synuclein in a bilayer determined by fluorescence, neutron reflectometry, and computation
    • Pfefferkorn, C. M., Heinrich, F., Sodt, A. J., Maltsev, A. S., Pastor, R. W., and Lee, J. C. (2012) Depth of a-synuclein in a bilayer determined by fluorescence, neutron reflectometry, and computation Biophys. J. 102, 613-621
    • (2012) Biophys. J. , vol.102 , pp. 613-621
    • Pfefferkorn, C.M.1    Heinrich, F.2    Sodt, A.J.3    Maltsev, A.S.4    Pastor, R.W.5    Lee, J.C.6
  • 25
    • 47749147652 scopus 로고    scopus 로고
    • Asymmetric structural features in single supported lipid bilayers containing cholesterol and GM1 resolved with synchrotron X-Ray reflectivity
    • Reich, C., Horton, M. R., Krause, B., Gast, A. P., Radler, J. O., and Nickel, B. (2008) Asymmetric structural features in single supported lipid bilayers containing cholesterol and GM1 resolved with synchrotron X-Ray reflectivity Biophys. J. 95, 657-668
    • (2008) Biophys. J. , vol.95 , pp. 657-668
    • Reich, C.1    Horton, M.R.2    Krause, B.3    Gast, A.P.4    Radler, J.O.5    Nickel, B.6
  • 26
    • 84881477828 scopus 로고    scopus 로고
    • Membrane bound α-synuclein is fully embedded in the lipid bilayer while segments with higher flexibility remain
    • Wietek, J., Haralampiev, I., Amoussouvi, A., Herrmann, A., and Stockl, M. (2013) Membrane bound α-synuclein is fully embedded in the lipid bilayer while segments with higher flexibility remain FEBS Lett. 587, 2572-2577
    • (2013) FEBS Lett. , vol.587 , pp. 2572-2577
    • Wietek, J.1    Haralampiev, I.2    Amoussouvi, A.3    Herrmann, A.4    Stockl, M.5
  • 27
    • 65449137602 scopus 로고    scopus 로고
    • Curvature dynamics of alpha-synuclein familial Parkinson disease mutants: Molecular simulations of the micelle- and bilayer-bound forms
    • Perlmutter, J. D., Braun, A. R., and Sachs, J. N. (2009) Curvature dynamics of alpha-synuclein familial Parkinson disease mutants: Molecular simulations of the micelle- and bilayer-bound forms J. Biol. Chem. 284, 7177-7189
    • (2009) J. Biol. Chem. , vol.284 , pp. 7177-7189
    • Perlmutter, J.D.1    Braun, A.R.2    Sachs, J.N.3
  • 29
    • 15744362063 scopus 로고    scopus 로고
    • Structure and dynamics of micelle-bound human alpha-synuclein
    • Ulmer, T. S., Bax, A., Cole, N. B., and Nussbaum, R. L. (2005) Structure and dynamics of micelle-bound human alpha-synuclein J. Biol. Chem. 280, 9595-9603
    • (2005) J. Biol. Chem. , vol.280 , pp. 9595-9603
    • Ulmer, T.S.1    Bax, A.2    Cole, N.B.3    Nussbaum, R.L.4
  • 30
    • 84880521916 scopus 로고    scopus 로고
    • α-Synuclein senses lipid packing defects and induces lateral expansion of lipids leading to membrane remodeling
    • Ouberai, M. M., Wang, J., Swann, M. J., Galvagnion, C., Guilliams, T., Dobson, C. M., and Welland, M. E. (2013) α-Synuclein senses lipid packing defects and induces lateral expansion of lipids leading to membrane remodeling J. Biol. Chem. 288, 20883-20895
    • (2013) J. Biol. Chem. , vol.288 , pp. 20883-20895
    • Ouberai, M.M.1    Wang, J.2    Swann, M.J.3    Galvagnion, C.4    Guilliams, T.5    Dobson, C.M.6    Welland, M.E.7
  • 31
    • 84865027786 scopus 로고    scopus 로고
    • Is adhesion superficial? Silicon wafers as a model system to study van der Waals interactions
    • Loskill, P., Hahl, H., Faidt, T., Grandthyll, S., Muller, F., and Jacobs, K. (2012) Is adhesion superficial? Silicon wafers as a model system to study van der Waals interactions Adv. Colloid Interfac 179-182, 107-13
    • (2012) Adv. Colloid Interfac , vol.179-182 , pp. 107-113
    • Loskill, P.1    Hahl, H.2    Faidt, T.3    Grandthyll, S.4    Muller, F.5    Jacobs, K.6
  • 33
    • 0141891097 scopus 로고    scopus 로고
    • The association of alpha-synuclein with membranes affects bilayer structure, stability, and fibril formation
    • Zhu, M., Li, J., and Fink, A. L. (2003) The association of alpha-synuclein with membranes affects bilayer structure, stability, and fibril formation J. Biol. Chem. 278, 40186-40197
    • (2003) J. Biol. Chem. , vol.278 , pp. 40186-40197
    • Zhu, M.1    Li, J.2    Fink, A.L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.