메뉴 건너뛰기




Volumn 106, Issue 3, 2014, Pages 556-565

Alpha-synuclein lipid-dependent membrane binding and translocation through the α-hemolysin channel

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA SYNUCLEIN; HEMOLYSIN; MEMBRANE LIPID;

EID: 84893473997     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1016/j.bpj.2013.12.028     Document Type: Article
Times cited : (28)

References (69)
  • 2
    • 0344808098 scopus 로고    scopus 로고
    • Immunoelectron-microscopic demonstration of NACP/α-synuclein- epitopes on the filamentous component of Lewy bodies in Parkinson's disease and in dementia with Lewy bodies
    • K. Arima, and K. Uéda M. Kawai Immunoelectron-microscopic demonstration of NACP/α-synuclein-epitopes on the filamentous component of Lewy bodies in Parkinson's disease and in dementia with Lewy bodies Brain Res. 808 1998 93 100
    • (1998) Brain Res. , vol.808 , pp. 93-100
    • Arima, K.1    Uéda, K.2    Kawai, M.3
  • 3
    • 0031715398 scopus 로고    scopus 로고
    • NACP/α-synuclein immunoreactivity in fibrillary components of neuronal and oligodendroglial cytoplasmic inclusions in the pontine nuclei in multiple system atrophy
    • K. Arima, and K. Uéda M. Kawai NACP/α-synuclein immunoreactivity in fibrillary components of neuronal and oligodendroglial cytoplasmic inclusions in the pontine nuclei in multiple system atrophy Acta Neuropathol. 96 1998 439 444
    • (1998) Acta Neuropathol. , vol.96 , pp. 439-444
    • Arima, K.1    Uéda, K.2    Kawai, M.3
  • 4
    • 0030744876 scopus 로고    scopus 로고
    • Mutation in the α-synuclein gene identified in families with Parkinson's disease
    • M.H. Polymeropoulos, and C. Lavedan R.L. Nussbaum Mutation in the α-synuclein gene identified in families with Parkinson's disease Science 276 1997 2045 2047
    • (1997) Science , vol.276 , pp. 2045-2047
    • Polymeropoulos, M.H.1    Lavedan, C.2    Nussbaum, R.L.3
  • 5
    • 0242300619 scopus 로고    scopus 로고
    • α-Synuclein locus triplication causes Parkinson's disease
    • A.B. Singleton, and M. Farrer K. Gwinn-Hardy α-Synuclein locus triplication causes Parkinson's disease Science 302 2003 841
    • (2003) Science , vol.302 , pp. 841
    • Singleton, A.B.1    Farrer, M.2    Gwinn-Hardy, K.3
  • 6
    • 4644290985 scopus 로고    scopus 로고
    • α-Synuclein locus duplication as a cause of familial Parkinson's disease
    • M.C. Chartier-Harlin, and J. Kachergus A. Destée α-Synuclein locus duplication as a cause of familial Parkinson's disease Lancet 364 2004 1167 1169
    • (2004) Lancet , vol.364 , pp. 1167-1169
    • Chartier-Harlin, M.C.1    Kachergus, J.2    Destée, A.3
  • 7
    • 77950521882 scopus 로고    scopus 로고
    • Absence of α-synuclein affects dopamine metabolism and synaptic markers in the striatum of aging mice
    • A. Al-Wandi, and N. Ninkina V.L. Buchman Absence of α-synuclein affects dopamine metabolism and synaptic markers in the striatum of aging mice Neurobiol. Aging 31 2010 796 804
    • (2010) Neurobiol. Aging , vol.31 , pp. 796-804
    • Al-Wandi, A.1    Ninkina, N.2    Buchman, V.L.3
  • 8
    • 77957347060 scopus 로고    scopus 로고
    • α-Synuclein promotes SNARE-complex assembly in vivo and in vitro
    • J. Burré, and M. Sharma T.C. Südhof α-Synuclein promotes SNARE-complex assembly in vivo and in vitro Science 329 2010 1663 1667
    • (2010) Science , vol.329 , pp. 1663-1667
    • Burré, J.1    Sharma, M.2    Südhof, T.C.3
  • 9
    • 0028277520 scopus 로고
    • Identification of two distinct synucleins from human brain
    • R. Jakes, M.G. Spillantini, and M. Goedert Identification of two distinct synucleins from human brain FEBS Lett. 345 1994 27 32
    • (1994) FEBS Lett. , vol.345 , pp. 27-32
    • Jakes, R.1    Spillantini, M.G.2    Goedert, M.3
  • 10
    • 2942555022 scopus 로고    scopus 로고
    • Structure of membrane-bound α-synuclein studied by site-directed spin labeling
    • C.C. Jao, and A. Der-Sarkissian R. Langen Structure of membrane-bound α-synuclein studied by site-directed spin labeling Proc. Natl. Acad. Sci. USA 101 2004 8331 8336
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 8331-8336
    • Jao, C.C.1    Der-Sarkissian, A.2    Langen, R.3
  • 11
    • 58149173445 scopus 로고    scopus 로고
    • Membrane-bound α-synuclein forms an extended helix: Long-distance pulsed ESR measurements using vesicles, bicelles, and rodlike micelles
    • E.R. Georgieva, and T.F. Ramlall D. Eliezer Membrane-bound α-synuclein forms an extended helix: long-distance pulsed ESR measurements using vesicles, bicelles, and rodlike micelles J. Am. Chem. Soc. 130 2008 12856 12857
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 12856-12857
    • Georgieva, E.R.1    Ramlall, T.F.2    Eliezer, D.3
  • 12
    • 58149380718 scopus 로고    scopus 로고
    • Structure of membrane-bound α-synuclein from site-directed spin labeling and computational refinement
    • C.C. Jao, and B.G. Hegde R. Langen Structure of membrane-bound α-synuclein from site-directed spin labeling and computational refinement Proc. Natl. Acad. Sci. USA 105 2008 19666 19671
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 19666-19671
    • Jao, C.C.1    Hegde, B.G.2    Langen, R.3
  • 13
    • 0032540327 scopus 로고    scopus 로고
    • Stabilization of α-synuclein secondary structure upon binding to synthetic membranes
    • W.S. Davidson, and A. Jonas J.M. George Stabilization of α-synuclein secondary structure upon binding to synthetic membranes J. Biol. Chem. 273 1998 9443 9449
    • (1998) J. Biol. Chem. , vol.273 , pp. 9443-9449
    • Davidson, W.S.1    Jonas, A.2    George, J.M.3
  • 14
    • 15744362063 scopus 로고    scopus 로고
    • Structure and dynamics of micelle-bound human α-synuclein
    • T.S. Ulmer, and A. Bax R.L. Nussbaum Structure and dynamics of micelle-bound human α-synuclein J. Biol. Chem. 280 2005 9595 9603
    • (2005) J. Biol. Chem. , vol.280 , pp. 9595-9603
    • Ulmer, T.S.1    Bax, A.2    Nussbaum, R.L.3
  • 15
    • 0038341134 scopus 로고    scopus 로고
    • A broken α-helix in folded α-synuclein
    • S. Chandra, and X.C. Chen T.C. Südhof A broken α-helix in folded α-synuclein J. Biol. Chem. 278 2003 15313 15318
    • (2003) J. Biol. Chem. , vol.278 , pp. 15313-15318
    • Chandra, S.1    Chen, X.C.2    Südhof, T.C.3
  • 16
    • 0035928748 scopus 로고    scopus 로고
    • Membrane binding and self-association of α-synucleins
    • V. Narayanan, and S. Scarlata Membrane binding and self-association of α-synucleins Biochemistry 40 2001 9927 9934
    • (2001) Biochemistry , vol.40 , pp. 9927-9934
    • Narayanan, V.1    Scarlata, S.2
  • 17
    • 77958455514 scopus 로고    scopus 로고
    • Effects of curvature and composition on α-synuclein binding to lipid vesicles
    • E.R. Middleton, and E. Rhoades Effects of curvature and composition on α-synuclein binding to lipid vesicles Biophys. J. 99 2010 2279 2288
    • (2010) Biophys. J. , vol.99 , pp. 2279-2288
    • Middleton, E.R.1    Rhoades, E.2
  • 18
    • 84893437757 scopus 로고    scopus 로고
    • Membrane remodeling by α-synuclein and effects on amyloid formation
    • Z. Jiang, M. de Messieres, and J.C. Lee Membrane remodeling by α-synuclein and effects on amyloid formation J. Am. Chem. Soc. 108 2013 56 64
    • (2013) J. Am. Chem. Soc. , vol.108 , pp. 56-64
    • Jiang, Z.1    De Messieres, M.2    Lee, J.C.3
  • 19
    • 84863012541 scopus 로고    scopus 로고
    • Depth of α-synuclein in a bilayer determined by fluorescence, neutron reflectometry, and computation
    • C.M. Pfefferkorn, and F. Heinrich J.C. Lee Depth of α-synuclein in a bilayer determined by fluorescence, neutron reflectometry, and computation Biophys. J. 102 2012 613 621
    • (2012) Biophys. J. , vol.102 , pp. 613-621
    • Pfefferkorn, C.M.1    Heinrich, F.2    Lee, J.C.3
  • 20
    • 58849088083 scopus 로고    scopus 로고
    • Clustering of α-synuclein on supported lipid bilayers: Role of anionic lipid, protein, and divalent ion concentration
    • A.P. Pandey, and F. Haque J.S. Hovis Clustering of α-synuclein on supported lipid bilayers: role of anionic lipid, protein, and divalent ion concentration Biophys. J. 96 2009 540 551
    • (2009) Biophys. J. , vol.96 , pp. 540-551
    • Pandey, A.P.1    Haque, F.2    Hovis, J.S.3
  • 21
    • 65549114936 scopus 로고    scopus 로고
    • Lipid bilayer disruption by oligomeric α-synuclein depends on bilayer charge and accessibility of the hydrophobic core
    • B.D. van Rooijen, M.M.A.E. Claessens, and V. Subramaniam Lipid bilayer disruption by oligomeric α-synuclein depends on bilayer charge and accessibility of the hydrophobic core Biochim. Biophys. Acta 1788 2009 1271 1278
    • (2009) Biochim. Biophys. Acta , vol.1788 , pp. 1271-1278
    • Van Rooijen, B.D.1    Claessens, M.M.A.E.2    Subramaniam, V.3
  • 22
    • 37249003742 scopus 로고    scopus 로고
    • Helical α-synuclein forms highly conductive ion channels
    • S.D. Zakharov, and J.D. Hulleman W.A. Cramer Helical α-synuclein forms highly conductive ion channels Biochemistry 46 2007 14369 14379
    • (2007) Biochemistry , vol.46 , pp. 14369-14379
    • Zakharov, S.D.1    Hulleman, J.D.2    Cramer, W.A.3
  • 23
    • 78650763561 scopus 로고    scopus 로고
    • Membrane permeabilization by oligomeric α-synuclein: In search of the mechanism
    • B.D. van Rooijen, M.M.A.E. Claessens, and V. Subramaniam Membrane permeabilization by oligomeric α-synuclein: in search of the mechanism PLoS ONE 5 2010 e14292
    • (2010) PLoS ONE , vol.5 , pp. 14292
    • Van Rooijen, B.D.1    Claessens, M.M.A.E.2    Subramaniam, V.3
  • 25
    • 0030447720 scopus 로고    scopus 로고
    • Structure of staphylococcal α-hemolysin, a heptameric transmembrane pore
    • L.Z. Song, and M.R. Hobaugh J.E. Gouaux Structure of staphylococcal α-hemolysin, a heptameric transmembrane pore Science 274 1996 1859 1866
    • (1996) Science , vol.274 , pp. 1859-1866
    • Song, L.Z.1    Hobaugh, M.R.2    Gouaux, J.E.3
  • 26
    • 0030384264 scopus 로고    scopus 로고
    • Dynamics and free energy of polymers partitioning into a nanoscale pore
    • S.M. Bezrukov, and I. Vodyanoy J.J. Kasianowicz Dynamics and free energy of polymers partitioning into a nanoscale pore Macromolecules 29 1996 8517 8522
    • (1996) Macromolecules , vol.29 , pp. 8517-8522
    • Bezrukov, S.M.1    Vodyanoy, I.2    Kasianowicz, J.J.3
  • 27
    • 0030465241 scopus 로고    scopus 로고
    • Characterization of individual polynucleotide molecules using a membrane channel
    • J.J. Kasianowicz, and E. Brandin D.W. Deamer Characterization of individual polynucleotide molecules using a membrane channel Proc. Natl. Acad. Sci. USA 93 1996 13770 13773
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 13770-13773
    • Kasianowicz, J.J.1    Brandin, E.2    Deamer, D.W.3
  • 28
    • 0033594410 scopus 로고    scopus 로고
    • Stochastic sensing of organic analytes by a pore-forming protein containing a molecular adapter
    • L.Q. Gu, and O. Braha H. Bayley Stochastic sensing of organic analytes by a pore-forming protein containing a molecular adapter Nature 398 1999 686 690
    • (1999) Nature , vol.398 , pp. 686-690
    • Gu, L.Q.1    Braha, O.2    Bayley, H.3
  • 29
    • 0033980542 scopus 로고    scopus 로고
    • Rapid nanopore discrimination between single polynucleotide molecules
    • A. Meller, and L. Nivon D. Branton Rapid nanopore discrimination between single polynucleotide molecules Proc. Natl. Acad. Sci. USA 97 2000 1079 1084
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 1079-1084
    • Meller, A.1    Nivon, L.2    Branton, D.3
  • 30
    • 16344373084 scopus 로고    scopus 로고
    • Field-dependent effect of crown ether (18-crown-6) on ionic conductance of α-hemolysin channels
    • S.M. Bezrukov, and O.V. Krasilnikov C.G. Rodrigues Field-dependent effect of crown ether (18-crown-6) on ionic conductance of α-hemolysin channels Biophys. J. 87 2004 3162 3171
    • (2004) Biophys. J. , vol.87 , pp. 3162-3171
    • Bezrukov, S.M.1    Krasilnikov, O.V.2    Rodrigues, C.G.3
  • 31
    • 77956424842 scopus 로고    scopus 로고
    • Nucleobase recognition in ssDNA at the central constriction of the α-hemolysin pore
    • D. Stoddart, and A.J. Heron H. Bayley Nucleobase recognition in ssDNA at the central constriction of the α-hemolysin pore Nano Lett. 10 2010 3633 3637
    • (2010) Nano Lett. , vol.10 , pp. 3633-3637
    • Stoddart, D.1    Heron, A.J.2    Bayley, H.3
  • 32
    • 84861722732 scopus 로고    scopus 로고
    • Nanopore analysis: An emerging technique for studying the folding and misfolding of proteins
    • C. Madampage, and O. Tavassoly J.S. Lee Nanopore analysis: an emerging technique for studying the folding and misfolding of proteins Prion 6 2012 116 123
    • (2012) Prion , vol.6 , pp. 116-123
    • Madampage, C.1    Tavassoly, O.2    Lee, J.S.3
  • 33
    • 84883471457 scopus 로고    scopus 로고
    • Analysis of a single α-synuclein fibrillation by the interaction with a protein nanopore
    • H.Y. Wang, and Z. Gu Y.T. Long Analysis of a single α-synuclein fibrillation by the interaction with a protein nanopore Anal. Chem. 85 2013 8254 8261
    • (2013) Anal. Chem. , vol.85 , pp. 8254-8261
    • Wang, H.Y.1    Gu, Z.2    Long, Y.T.3
  • 34
    • 0025854858 scopus 로고
    • A protein-conducting channel in the endoplasmic reticulum
    • S.M. Simon, and G. Blobel A protein-conducting channel in the endoplasmic reticulum Cell 65 1991 371 380
    • (1991) Cell , vol.65 , pp. 371-380
    • Simon, S.M.1    Blobel, G.2
  • 36
    • 0031714548 scopus 로고    scopus 로고
    • The diphtheria toxin channel-forming T domain translocates its own NH2-terminal region across planar bilayers
    • L. Senzel, and P.D. Huynh A. Finkelstein The diphtheria toxin channel-forming T domain translocates its own NH2-terminal region across planar bilayers J. Gen. Physiol. 112 1998 317 324
    • (1998) J. Gen. Physiol. , vol.112 , pp. 317-324
    • Senzel, L.1    Huynh, P.D.2    Finkelstein, A.3
  • 37
    • 0033776881 scopus 로고    scopus 로고
    • Protein translocation across planar bilayers by the colicin Ia channel-forming domain: Where will it end?
    • P.K. Kienker, K.S. Jakes, and A. Finkelstein Protein translocation across planar bilayers by the colicin Ia channel-forming domain: where will it end? J. Gen. Physiol. 116 2000 587 598
    • (2000) J. Gen. Physiol. , vol.116 , pp. 587-598
    • Kienker, P.K.1    Jakes, K.S.2    Finkelstein, A.3
  • 38
    • 10044247127 scopus 로고    scopus 로고
    • Evidence that translocation of anthrax toxin's lethal factor is initiated by entry of its N terminus into the protective antigen channel
    • S. Zhang, A. Finkelstein, and R.J. Collier Evidence that translocation of anthrax toxin's lethal factor is initiated by entry of its N terminus into the protective antigen channel Proc. Natl. Acad. Sci. USA 101 2004 16756 16761
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 16756-16761
    • Zhang, S.1    Finkelstein, A.2    Collier, R.J.3
  • 39
    • 23044508996 scopus 로고    scopus 로고
    • A phenylalanine clamp catalyzes protein translocation through the anthrax toxin pore
    • B.A. Krantz, and R.A. Melnyk R.J. Collier A phenylalanine clamp catalyzes protein translocation through the anthrax toxin pore Science 309 2005 777 781
    • (2005) Science , vol.309 , pp. 777-781
    • Krantz, B.A.1    Melnyk, R.A.2    Collier, R.J.3
  • 40
    • 61449324931 scopus 로고    scopus 로고
    • Proton-coupled protein transport through the anthrax toxin channel
    • A. Finkelstein Proton-coupled protein transport through the anthrax toxin channel Philos. Trans. R. Soc. Lond. B Biol. Sci. 364 2009 209 215
    • (2009) Philos. Trans. R. Soc. Lond. B Biol. Sci. , vol.364 , pp. 209-215
    • Finkelstein, A.1
  • 41
    • 78149459196 scopus 로고    scopus 로고
    • Facilitated translocation of polypeptides through a single nanopore
    • R. Bikwemu, and A.J. Wolfe L. Movileanu Facilitated translocation of polypeptides through a single nanopore J. Phys. Condens Mat. 22 2010 454117
    • (2010) J. Phys. Condens Mat. , vol.22 , pp. 454117
    • Bikwemu, R.1    Wolfe, A.J.2    Movileanu, L.3
  • 42
    • 84860200742 scopus 로고    scopus 로고
    • Ratcheting up protein translocation with anthrax toxin
    • G.K. Feld, M.J. Brown, and B.A. Krantz Ratcheting up protein translocation with anthrax toxin Protein Sci. 21 2012 606 624
    • (2012) Protein Sci. , vol.21 , pp. 606-624
    • Feld, G.K.1    Brown, M.J.2    Krantz, B.A.3
  • 44
    • 84876412824 scopus 로고    scopus 로고
    • Multistep protein unfolding during nanopore translocation
    • D. Rodriguez-Larrea, and H. Bayley Multistep protein unfolding during nanopore translocation Nat. Nanotechnol. 8 2013 288 295
    • (2013) Nat. Nanotechnol. , vol.8 , pp. 288-295
    • Rodriguez-Larrea, D.1    Bayley, H.2
  • 45
    • 84879672979 scopus 로고    scopus 로고
    • Intrinsically disordered protein threads through the bacterial outer-membrane porin OmpF
    • N.G. Housden, and J.T. Hopper C. Kleanthous Intrinsically disordered protein threads through the bacterial outer-membrane porin OmpF Science 340 2013 1570 1574
    • (2013) Science , vol.340 , pp. 1570-1574
    • Housden, N.G.1    Hopper, J.T.2    Kleanthous, C.3
  • 46
    • 4143112232 scopus 로고    scopus 로고
    • Structure of peptides investigated by nanopore analysis
    • T.C. Sutherland, and Y.T. Long J.S. Lee Structure of peptides investigated by nanopore analysis Nano Lett. 4 2004 1273 1277
    • (2004) Nano Lett. , vol.4 , pp. 1273-1277
    • Sutherland, T.C.1    Long, Y.T.2    Lee, J.S.3
  • 47
    • 34147108667 scopus 로고    scopus 로고
    • Unfolding of proteins and long transient conformations detected by single nanopore recording
    • G. Oukhaled, and J. Mathé L. Auvray Unfolding of proteins and long transient conformations detected by single nanopore recording Phys. Rev. Lett. 98 2007 158101
    • (2007) Phys. Rev. Lett. , vol.98 , pp. 158101
    • Oukhaled, G.1    Mathé, J.2    Auvray, L.3
  • 48
    • 84875153533 scopus 로고    scopus 로고
    • Unfoldase-mediated protein translocation through an α-hemolysin nanopore
    • J. Nivala, D.B. Marks, and M. Akeson Unfoldase-mediated protein translocation through an α-hemolysin nanopore Nat. Biotechnol. 31 2013 247 250
    • (2013) Nat. Biotechnol. , vol.31 , pp. 247-250
    • Nivala, J.1    Marks, D.B.2    Akeson, M.3
  • 50
    • 79952271938 scopus 로고    scopus 로고
    • Dynamics of unfolded protein transport through an aerolysin pore
    • M. Pastoriza-Gallego, and L. Rabah J. Pelta Dynamics of unfolded protein transport through an aerolysin pore J. Am. Chem. Soc. 133 2011 2923 2931
    • (2011) J. Am. Chem. Soc. , vol.133 , pp. 2923-2931
    • Pastoriza-Gallego, M.1    Rabah, L.2    Pelta, J.3
  • 51
    • 58149402384 scopus 로고    scopus 로고
    • Enhanced translocation of single DNA molecules through α-hemolysin nanopores by manipulation of internal charge
    • G. Maglia, and M.R. Restrepo H. Bayley Enhanced translocation of single DNA molecules through α-hemolysin nanopores by manipulation of internal charge Proc. Natl. Acad. Sci. USA 105 2008 19720 19725
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 19720-19725
    • Maglia, G.1    Restrepo, M.R.2    Bayley, H.3
  • 52
    • 67650069570 scopus 로고    scopus 로고
    • The dynamic side of the Hofmeister effect: A single-molecule nanopore study of specific complex formation
    • P.A. Gurnev, and D. Harries S.M. Bezrukov The dynamic side of the Hofmeister effect: a single-molecule nanopore study of specific complex formation ChemPhysChem 10 2009 1445 1449
    • (2009) ChemPhysChem , vol.10 , pp. 1445-1449
    • Gurnev, P.A.1    Harries, D.2    Bezrukov, S.M.3
  • 53
    • 77950559887 scopus 로고    scopus 로고
    • Tryptophan probes at the α-synuclein and membrane interface
    • C.M. Pfefferkorn, and J.C. Lee Tryptophan probes at the α-synuclein and membrane interface J. Phys. Chem. B 114 2010 4615 4622
    • (2010) J. Phys. Chem. B , vol.114 , pp. 4615-4622
    • Pfefferkorn, C.M.1    Lee, J.C.2
  • 54
    • 0034319631 scopus 로고    scopus 로고
    • Particle number fluctuations in a membrane channel
    • S.M. Bezrukov, and A.M. Berezhkovskii A. Szabo Particle number fluctuations in a membrane channel J. Chem. Phys. 113 2000 8206 8211
    • (2000) J. Chem. Phys. , vol.113 , pp. 8206-8211
    • Bezrukov, S.M.1    Berezhkovskii, A.M.2    Szabo, A.3
  • 55
    • 34648813938 scopus 로고    scopus 로고
    • Diffusion model of solute dynamics in a membrane channel: Mapping onto the two-site model and optimizing the flux
    • S.M. Bezrukov, A.M. Berezhkovskii, and A. Szabo Diffusion model of solute dynamics in a membrane channel: mapping onto the two-site model and optimizing the flux J. Chem. Phys. 127 2007 115101
    • (2007) J. Chem. Phys. , vol.127 , pp. 115101
    • Bezrukov, S.M.1    Berezhkovskii, A.M.2    Szabo, A.3
  • 56
    • 38949139507 scopus 로고    scopus 로고
    • Conformational equilibria in monomeric α-synuclein at the single-molecule level
    • M. Sandal, and F. Valle B. Samorì Conformational equilibria in monomeric α-synuclein at the single-molecule level PLoS Biol. 6 2008 e6
    • (2008) PLoS Biol. , vol.6 , pp. 6
    • Sandal, M.1    Valle, F.2    Samorì, B.3
  • 57
    • 77950659588 scopus 로고    scopus 로고
    • Early aggregation steps in α-synuclein as measured by FCS and FRET: Evidence for a contagious conformational change
    • S. Nath, and J. Meuvis Y. Engelborghs Early aggregation steps in α-synuclein as measured by FCS and FRET: evidence for a contagious conformational change Biophys. J. 98 2010 1302 1311
    • (2010) Biophys. J. , vol.98 , pp. 1302-1311
    • Nath, S.1    Meuvis, J.2    Engelborghs, Y.3
  • 58
    • 84865472739 scopus 로고    scopus 로고
    • Membrane lipid composition regulates tubulin interaction with mitochondrial voltage-dependent anion channel
    • T.K. Rostovtseva, and P.A. Gurnev S.M. Bezrukov Membrane lipid composition regulates tubulin interaction with mitochondrial voltage-dependent anion channel J. Biol. Chem. 287 2012 29589 29598
    • (2012) J. Biol. Chem. , vol.287 , pp. 29589-29598
    • Rostovtseva, T.K.1    Gurnev, P.A.2    Bezrukov, S.M.3
  • 59
    • 0015879604 scopus 로고
    • Ionic blockage of sodium channels in nerve
    • A.M. Woodhull Ionic blockage of sodium channels in nerve J. Gen. Physiol. 61 1973 687 708
    • (1973) J. Gen. Physiol. , vol.61 , pp. 687-708
    • Woodhull, A.M.1
  • 60
    • 0025225339 scopus 로고
    • Voltage-dependent block of anthrax toxin channels in planar phospholipid bilayer membranes by symmetric tetraalkylammonium ions. Single-channel analysis
    • R.O. Blaustein, E.J.A. Lea, and A. Finkelstein Voltage-dependent block of anthrax toxin channels in planar phospholipid bilayer membranes by symmetric tetraalkylammonium ions. Single-channel analysis J. Gen. Physiol. 96 1990 921 942
    • (1990) J. Gen. Physiol. , vol.96 , pp. 921-942
    • Blaustein, R.O.1    Lea, E.J.A.2    Finkelstein, A.3
  • 61
    • 0031973867 scopus 로고    scopus 로고
    • Voltage dependence of open channel blockade: Onset and offset rates
    • D.B. Tikhonov, and L.G. Magazanik Voltage dependence of open channel blockade: onset and offset rates J. Membr. Biol. 161 1998 1 8
    • (1998) J. Membr. Biol. , vol.161 , pp. 1-8
    • Tikhonov, D.B.1    Magazanik, L.G.2
  • 62
    • 36148943499 scopus 로고    scopus 로고
    • Catalyzing the translocation of polypeptides through attractive interactions
    • A.J. Wolfe, and M.M. Mohammad L. Movileanu Catalyzing the translocation of polypeptides through attractive interactions J. Am. Chem. Soc. 129 2007 14034 14041
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 14034-14041
    • Wolfe, A.J.1    Mohammad, M.M.2    Movileanu, L.3
  • 63
    • 77954345106 scopus 로고    scopus 로고
    • Blockage of anthrax PA63 pore by a multicharged high-affinity toxin inhibitor
    • E.M. Nestorovich, and V.A. Karginov S.M. Bezrukov Blockage of anthrax PA63 pore by a multicharged high-affinity toxin inhibitor Biophys. J. 99 2010 134 143
    • (2010) Biophys. J. , vol.99 , pp. 134-143
    • Nestorovich, E.M.1    Karginov, V.A.2    Bezrukov, S.M.3
  • 64
    • 58149360789 scopus 로고    scopus 로고
    • Mechanism of KCl enhancement in detection of nonionic polymers by nanopore sensors
    • C.G. Rodrigues, and D.C. Machado O.V. Krasilnikov Mechanism of KCl enhancement in detection of nonionic polymers by nanopore sensors Biophys. J. 95 2008 5186 5192
    • (2008) Biophys. J. , vol.95 , pp. 5186-5192
    • Rodrigues, C.G.1    Machado, D.C.2    Krasilnikov, O.V.3
  • 65
    • 0041376917 scopus 로고    scopus 로고
    • Channel-facilitated membrane transport: Average lifetimes in the channel
    • A.M. Berezhkovskii, M.A. Pustovoit, and S.M. Bezrukov Channel-facilitated membrane transport: average lifetimes in the channel J. Chem. Phys. 119 2003 3943 3951
    • (2003) J. Chem. Phys. , vol.119 , pp. 3943-3951
    • Berezhkovskii, A.M.1    Pustovoit, M.A.2    Bezrukov, S.M.3
  • 66
    • 78149421728 scopus 로고    scopus 로고
    • Osmotic stress regulates the strength and kinetics of sugar binding to the maltoporin channel
    • P.A. Gurnev, and D. Harries S.M. Bezrukov Osmotic stress regulates the strength and kinetics of sugar binding to the maltoporin channel J. Phys. Condens Mat. 22 2010 454110
    • (2010) J. Phys. Condens Mat. , vol.22 , pp. 454110
    • Gurnev, P.A.1    Harries, D.2    Bezrukov, S.M.3
  • 67
    • 0033582763 scopus 로고    scopus 로고
    • Single molecule force spectroscopy of spectrin repeats: Low unfolding forces in helix bundles
    • M. Rief, and J. Pascual H.E. Gaub Single molecule force spectroscopy of spectrin repeats: low unfolding forces in helix bundles J. Mol. Biol. 286 1999 553 561
    • (1999) J. Mol. Biol. , vol.286 , pp. 553-561
    • Rief, M.1    Pascual, J.2    Gaub, H.E.3
  • 68
    • 84865355673 scopus 로고    scopus 로고
    • Effect of the compatible solute ectoine on the stability of the membrane proteins
    • A. Roychoudhury, D. Haussinger, and F. Oesterhelt Effect of the compatible solute ectoine on the stability of the membrane proteins Protein Pept. Lett. 19 2012 791 794
    • (2012) Protein Pept. Lett. , vol.19 , pp. 791-794
    • Roychoudhury, A.1    Haussinger, D.2    Oesterhelt, F.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.