메뉴 건너뛰기




Volumn 103, Issue 7, 2012, Pages 1500-1509

β-amyloid (1-40) peptide interactions with supported phospholipid membranes: A single-molecule study

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID BETA PROTEIN; AMYLOID BETA PROTEIN[1-40]; PEPTIDE FRAGMENT; PHOSPHOLIPID;

EID: 84866995239     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1016/j.bpj.2012.08.051     Document Type: Article
Times cited : (55)

References (56)
  • 1
    • 0028856460 scopus 로고
    • An English translation of Alzheimer's 1907 paper, "uber eine eigenartige Erkankung der Hirnrinde"
    • A. Alzheimer, and R.A. Stelzmann F.R. Murtagh An English translation of Alzheimer's 1907 paper, "Uber eine eigenartige Erkankung der Hirnrinde" Clin. Anat. 8 1995 429 431
    • (1995) Clin. Anat. , vol.8 , pp. 429-431
    • Alzheimer, A.1    Stelzmann, R.A.2    Murtagh, F.R.3
  • 2
    • 37049048544 scopus 로고
    • Paired helical filaments in electron microscopy of Alzheimer's disease
    • M. Kidd Paired helical filaments in electron microscopy of Alzheimer's disease Nature 197 1963 192 193
    • (1963) Nature , vol.197 , pp. 192-193
    • Kidd, M.1
  • 3
    • 78651158156 scopus 로고
    • Ultrastructural studies in Alzheimer's presenile dementia
    • R.D. Terry, N.K. Gonatas, and M. Weiss Ultrastructural studies in Alzheimer's presenile dementia Am. J. Pathol. 44 1964 269 297
    • (1964) Am. J. Pathol. , vol.44 , pp. 269-297
    • Terry, R.D.1    Gonatas, N.K.2    Weiss, M.3
  • 4
    • 0021256895 scopus 로고
    • Alzheimer's disease: Initial report of the purification and characterization of a novel cerebrovascular amyloid protein
    • G.G. Glenner, and C.W. Wong Alzheimer's disease: initial report of the purification and characterization of a novel cerebrovascular amyloid protein Biochem. Biophys. Res. Commun. 120 1984 885 890
    • (1984) Biochem. Biophys. Res. Commun. , vol.120 , pp. 885-890
    • Glenner, G.G.1    Wong, C.W.2
  • 5
    • 0022654027 scopus 로고
    • Isolation of low-molecular-weight proteins from amyloid plaque fibers in Alzheimer's disease
    • D.J. Selkoe, and C.R. Abraham L.K. Duffy Isolation of low-molecular-weight proteins from amyloid plaque fibers in Alzheimer's disease J. Neurochem. 46 1986 1820 1834
    • (1986) J. Neurochem. , vol.46 , pp. 1820-1834
    • Selkoe, D.J.1    Abraham, C.R.2    Duffy, L.K.3
  • 6
    • 0012510759 scopus 로고
    • Amyloid plaque core protein in Alzheimer disease and Down syndrome
    • C.L. Masters, and G. Simms K. Beyreuther Amyloid plaque core protein in Alzheimer disease and Down syndrome Proc. Natl. Acad. Sci. USA 82 1985 4245 4249
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 4245-4249
    • Masters, C.L.1    Simms, G.2    Beyreuther, K.3
  • 7
    • 0034716942 scopus 로고    scopus 로고
    • Direct visualisation of the beta-sheet structure of synthetic Alzheimer's amyloid
    • L.C. Serpell, and J.M. Smith Direct visualisation of the beta-sheet structure of synthetic Alzheimer's amyloid J. Mol. Biol. 299 2000 225 231
    • (2000) J. Mol. Biol. , vol.299 , pp. 225-231
    • Serpell, L.C.1    Smith, J.M.2
  • 8
    • 28444442999 scopus 로고    scopus 로고
    • 3D structure of Alzheimer's amyloid-beta(1-42) fibrils
    • T. Lührs, and C. Ritter R. Riek 3D structure of Alzheimer's amyloid-beta(1-42) fibrils Proc. Natl. Acad. Sci. USA 102 2005 17342 17347
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 17342-17347
    • Lührs, T.1    Ritter, C.2    Riek, R.3
  • 9
    • 0032888131 scopus 로고    scopus 로고
    • Soluble amyloid beta peptide concentration as a predictor of synaptic change in Alzheimer's disease
    • L.F. Lue, and Y.M. Kuo J. Rogers Soluble amyloid beta peptide concentration as a predictor of synaptic change in Alzheimer's disease Am. J. Pathol. 155 1999 853 862
    • (1999) Am. J. Pathol. , vol.155 , pp. 853-862
    • Lue, L.F.1    Kuo, Y.M.2    Rogers, J.3
  • 10
    • 0028915895 scopus 로고
    • Amyloid beta protein (A beta) in Alzheimer's disease brain. Biochemical and immunocytochemical analysis with antibodies specific for forms ending at A beta 40 or A beta 42(43)
    • S.A. Gravina, and L. Ho S.G. Younkin Amyloid beta protein (A beta) in Alzheimer's disease brain. Biochemical and immunocytochemical analysis with antibodies specific for forms ending at A beta 40 or A beta 42(43) J. Biol. Chem. 270 1995 7013 7016
    • (1995) J. Biol. Chem. , vol.270 , pp. 7013-7016
    • Gravina, S.A.1    Ho, L.2    Younkin, S.G.3
  • 11
    • 0026794746 scopus 로고
    • Mass spectrometry of purified amyloid beta protein in Alzheimer's disease
    • H. Mori, and K. Takio D.J. Selkoe Mass spectrometry of purified amyloid beta protein in Alzheimer's disease J. Biol. Chem. 267 1992 17082 17086
    • (1992) J. Biol. Chem. , vol.267 , pp. 17082-17086
    • Mori, H.1    Takio, K.2    Selkoe, D.J.3
  • 12
    • 0027332081 scopus 로고
    • Beta-Amyloid-(1-42) is a major component of cerebrovascular amyloid deposits: Implications for the pathology of Alzheimer disease
    • A.E. Roher, and J.D. Lowenson M.J. Ball beta-Amyloid-(1-42) is a major component of cerebrovascular amyloid deposits: implications for the pathology of Alzheimer disease Proc. Natl. Acad. Sci. USA 90 1993 10836 10840
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 10836-10840
    • Roher, A.E.1    Lowenson, J.D.2    Ball, M.J.3
  • 13
    • 0025899041 scopus 로고
    • Amyloid deposition as the central event in the aetiology of Alzheimer's disease
    • J. Hardy, and D. Allsop Amyloid deposition as the central event in the aetiology of Alzheimer's disease Trends Pharmacol. Sci. 12 1991 383 388
    • (1991) Trends Pharmacol. Sci. , vol.12 , pp. 383-388
    • Hardy, J.1    Allsop, D.2
  • 14
    • 0036150827 scopus 로고    scopus 로고
    • Alzheimer's disease-do tauists and baptists finally shake hands?
    • A. Mudher, and S. Lovestone Alzheimer's disease-do tauists and baptists finally shake hands? Trends Neurosci. 25 2002 22 26
    • (2002) Trends Neurosci. , vol.25 , pp. 22-26
    • Mudher, A.1    Lovestone, S.2
  • 15
    • 20444496481 scopus 로고    scopus 로고
    • Calcium dysregulation and membrane disruption as a ubiquitous neurotoxic mechanism of soluble amyloid oligomers
    • A. Demuro, and E. Mina C.G. Glabe Calcium dysregulation and membrane disruption as a ubiquitous neurotoxic mechanism of soluble amyloid oligomers J. Biol. Chem. 280 2005 17294 17300
    • (2005) J. Biol. Chem. , vol.280 , pp. 17294-17300
    • Demuro, A.1    Mina, E.2    Glabe, C.G.3
  • 16
    • 0036369164 scopus 로고    scopus 로고
    • Heterogeneous amyloid-formed ion channels as a common cytotoxic mechanism: Implications for therapeutic strategies against amyloidosis
    • J.I. Kourie, and A.L. Culverson K.N. Laohachai Heterogeneous amyloid-formed ion channels as a common cytotoxic mechanism: implications for therapeutic strategies against amyloidosis Cell Biochem. Biophys. 36 2002 191 207
    • (2002) Cell Biochem. Biophys. , vol.36 , pp. 191-207
    • Kourie, J.I.1    Culverson, A.L.2    Laohachai, K.N.3
  • 17
    • 0035159553 scopus 로고    scopus 로고
    • Amyloid beta protein forms ion channels: Implications for Alzheimer's disease pathophysiology
    • H. Lin, R. Bhatia, and R. Lal Amyloid beta protein forms ion channels: implications for Alzheimer's disease pathophysiology FASEB J. 15 2001 2433 2444
    • (2001) FASEB J. , vol.15 , pp. 2433-2444
    • Lin, H.1    Bhatia, R.2    Lal, R.3
  • 18
    • 0027490362 scopus 로고
    • Giant multilevel cation channels formed by Alzheimer disease amyloid beta-protein [A beta P-(1-40)] in bilayer membranes
    • N. Arispe, H.B. Pollard, and E. Rojas Giant multilevel cation channels formed by Alzheimer disease amyloid beta-protein [A beta P-(1-40)] in bilayer membranes Proc. Natl. Acad. Sci. USA 90 1993 10573 10577
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 10573-10577
    • Arispe, N.1    Pollard, H.B.2    Rojas, E.3
  • 19
    • 49149124343 scopus 로고    scopus 로고
    • Amyloid-beta protein dimers isolated directly from Alzheimer's brains impair synaptic plasticity and memory
    • G.M. Shankar, and S. Li D.J. Selkoe Amyloid-beta protein dimers isolated directly from Alzheimer's brains impair synaptic plasticity and memory Nat. Med. 14 2008 837 842
    • (2008) Nat. Med. , vol.14 , pp. 837-842
    • Shankar, G.M.1    Li, S.2    Selkoe, D.J.3
  • 20
    • 42949155299 scopus 로고    scopus 로고
    • Amyloid beta protein dimer-containing human CSF disrupts synaptic plasticity: Prevention by systemic passive immunization
    • I. Klyubin, and V. Betts M.J. Rowan Amyloid beta protein dimer-containing human CSF disrupts synaptic plasticity: prevention by systemic passive immunization J. Neurosci. 28 2008 4231 4237
    • (2008) J. Neurosci. , vol.28 , pp. 4231-4237
    • Klyubin, I.1    Betts, V.2    Rowan, M.J.3
  • 22
    • 23044449398 scopus 로고    scopus 로고
    • Amyloid ion channels: A common structural link for protein-misfolding disease
    • A. Quist, and I. Doudevski R. Lal Amyloid ion channels: a common structural link for protein-misfolding disease Proc. Natl. Acad. Sci. USA 102 2005 10427 10432
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 10427-10432
    • Quist, A.1    Doudevski, I.2    Lal, R.3
  • 23
    • 58549084816 scopus 로고    scopus 로고
    • Amyloid-beta membrane binding and permeabilization are distinct processes influenced separately by membrane charge and fluidity
    • P.T. Wong, and J.A. Schauerte A. Gafni Amyloid-beta membrane binding and permeabilization are distinct processes influenced separately by membrane charge and fluidity J. Mol. Biol. 386 2009 81 96
    • (2009) J. Mol. Biol. , vol.386 , pp. 81-96
    • Wong, P.T.1    Schauerte, J.A.2    Gafni, A.3
  • 24
    • 0028179865 scopus 로고
    • Alzheimer beta-amyloid peptide 25-35: Electrostatic interactions with phospholipid membranes
    • E. Terzi, G. Hölzemann, and J. Seelig Alzheimer beta-amyloid peptide 25-35: electrostatic interactions with phospholipid membranes Biochemistry 33 1994 7434 7441
    • (1994) Biochemistry , vol.33 , pp. 7434-7441
    • Terzi, E.1    Hölzemann, G.2    Seelig, J.3
  • 25
    • 0028982292 scopus 로고
    • Self-association of beta-amyloid peptide (1-40) in solution and binding to lipid membranes
    • E. Terzi, G. Hölzemann, and J. Seelig Self-association of beta-amyloid peptide (1-40) in solution and binding to lipid membranes J. Mol. Biol. 252 1995 633 642
    • (1995) J. Mol. Biol. , vol.252 , pp. 633-642
    • Terzi, E.1    Hölzemann, G.2    Seelig, J.3
  • 26
    • 0030892291 scopus 로고    scopus 로고
    • Characterization of the interactions of Alzheimer beta-amyloid peptides with phospholipid membranes
    • J. McLaurin, and A. Chakrabartty Characterization of the interactions of Alzheimer beta-amyloid peptides with phospholipid membranes Eur. J. Biochem. 245 1997 355 363
    • (1997) Eur. J. Biochem. , vol.245 , pp. 355-363
    • McLaurin, J.1    Chakrabartty, A.2
  • 27
    • 0033569981 scopus 로고    scopus 로고
    • Structure of the Alzheimer beta-amyloid peptide (25-35) and its interaction with negatively charged phospholipid vesicles
    • M. Del Mar Martínez-Senac, J. Villalaín, and J.C. Gómez-Fernández Structure of the Alzheimer beta-amyloid peptide (25-35) and its interaction with negatively charged phospholipid vesicles Eur. J. Biochem. 265 1999 744 753
    • (1999) Eur. J. Biochem. , vol.265 , pp. 744-753
    • Del Mar Martínez-Senac, M.1    Villalaín, J.2    Gómez- Fernández, J.C.3
  • 28
    • 0347753786 scopus 로고    scopus 로고
    • Two types of Alzheimer's beta-amyloid (1-40) peptide membrane interactions: Aggregation preventing transmembrane anchoring versus accelerated surface fibril formation
    • M. Bokvist, and F. Lindström G. Gröbner Two types of Alzheimer's beta-amyloid (1-40) peptide membrane interactions: aggregation preventing transmembrane anchoring versus accelerated surface fibril formation J. Mol. Biol. 335 2004 1039 1049
    • (2004) J. Mol. Biol. , vol.335 , pp. 1039-1049
    • Bokvist, M.1    Lindström, F.2    Gröbner, G.3
  • 29
    • 4444328762 scopus 로고    scopus 로고
    • Insertion of Alzheimer's A beta 40 peptide into lipid monolayers
    • C. Ege, and K.Y.C. Lee Insertion of Alzheimer's A beta 40 peptide into lipid monolayers Biophys. J. 87 2004 1732 1740
    • (2004) Biophys. J. , vol.87 , pp. 1732-1740
    • Ege, C.1    Lee, K.Y.C.2
  • 30
    • 42749095305 scopus 로고    scopus 로고
    • Driving force of binding of amyloid beta-protein to lipid bilayers
    • K. Ikeda, and K. Matsuzaki Driving force of binding of amyloid beta-protein to lipid bilayers Biochem. Biophys. Res. Commun. 370 2008 525 529
    • (2008) Biochem. Biophys. Res. Commun. , vol.370 , pp. 525-529
    • Ikeda, K.1    Matsuzaki, K.2
  • 31
    • 0035942997 scopus 로고    scopus 로고
    • Profile of changes in lipid bilayer structure caused by beta-amyloid peptide
    • J.J. Kremer, D.J. Sklansky, and R.M. Murphy Profile of changes in lipid bilayer structure caused by beta-amyloid peptide Biochemistry 40 2001 8563 8571
    • (2001) Biochemistry , vol.40 , pp. 8563-8571
    • Kremer, J.J.1    Sklansky, D.J.2    Murphy, R.M.3
  • 32
    • 77953372048 scopus 로고    scopus 로고
    • Cytotoxic effects of GM1 ganglioside and amyloid b-peptide on mouse embryonic neural stem cells
    • M. Yanagisawa, T. Ariga, and R.K. Yu Cytotoxic effects of GM1 ganglioside and amyloid b-peptide on mouse embryonic neural stem cells ASN Neuro 2 2010 49 56
    • (2010) ASN Neuro , vol.2 , pp. 49-56
    • Yanagisawa, M.1    Ariga, T.2    Yu, R.K.3
  • 33
    • 33748792254 scopus 로고    scopus 로고
    • Beta-Amyloid-induced dynamin 1 degradation is mediated by N-methyl-D-aspartate receptors in hippocampal neurons
    • B.L. Kelly, and A. Ferreira beta-Amyloid-induced dynamin 1 degradation is mediated by N-methyl-D-aspartate receptors in hippocampal neurons J. Biol. Chem. 281 2006 28079 28089
    • (2006) J. Biol. Chem. , vol.281 , pp. 28079-28089
    • Kelly, B.L.1    Ferreira, A.2
  • 34
    • 57649223693 scopus 로고    scopus 로고
    • Nonspecific interaction of prefibrillar amyloid aggregates with glutamatergic receptors results in Ca2+ increase in primary neuronal cells
    • F. Pellistri, and M. Bucciantini M. Stefani Nonspecific interaction of prefibrillar amyloid aggregates with glutamatergic receptors results in Ca2+ increase in primary neuronal cells J. Biol. Chem. 283 2008 29950 29960
    • (2008) J. Biol. Chem. , vol.283 , pp. 29950-29960
    • Pellistri, F.1    Bucciantini, M.2    Stefani, M.3
  • 35
    • 84857642949 scopus 로고    scopus 로고
    • The toxic Aβ oligomer and Alzheimer's disease: An emperor in need of clothes
    • I. Benilova, E. Karran, and B. De Strooper The toxic Aβ oligomer and Alzheimer's disease: an emperor in need of clothes Nat. Neurosci. 15 2012 349 357
    • (2012) Nat. Neurosci. , vol.15 , pp. 349-357
    • Benilova, I.1    Karran, E.2    De Strooper, B.3
  • 36
    • 75349097530 scopus 로고    scopus 로고
    • A causative link between the structure of aberrant protein oligomers and their toxicity
    • S. Campioni, and B. Mannini F. Chiti A causative link between the structure of aberrant protein oligomers and their toxicity Nat. Chem. Biol. 6 2010 140 147
    • (2010) Nat. Chem. Biol. , vol.6 , pp. 140-147
    • Campioni, S.1    Mannini, B.2    Chiti, F.3
  • 37
    • 0034713831 scopus 로고    scopus 로고
    • Action of antimicrobial peptides: Two-state model
    • H.W. Huang Action of antimicrobial peptides: two-state model Biochemistry 39 2000 8347 8352
    • (2000) Biochemistry , vol.39 , pp. 8347-8352
    • Huang, H.W.1
  • 38
    • 33748950268 scopus 로고    scopus 로고
    • Molecular mechanism of antimicrobial peptides: The origin of cooperativity
    • H.W. Huang Molecular mechanism of antimicrobial peptides: the origin of cooperativity Biochim. Biophys. Acta 1758 2006 1292 1302
    • (2006) Biochim. Biophys. Acta , vol.1758 , pp. 1292-1302
    • Huang, H.W.1
  • 40
    • 0034760118 scopus 로고    scopus 로고
    • Total internal reflection fluorescence microscopy in cell biology
    • D. Axelrod Total internal reflection fluorescence microscopy in cell biology Traffic 2 2001 764 774
    • (2001) Traffic , vol.2 , pp. 764-774
    • Axelrod, D.1
  • 41
    • 0041876386 scopus 로고    scopus 로고
    • Methods of single-molecule fluorescence spectroscopy and microscopy
    • W.E. Moerner, and D.P. Fromm Methods of single-molecule fluorescence spectroscopy and microscopy Rev. Sci. Instrum. 74 2003 3597 3619
    • (2003) Rev. Sci. Instrum. , vol.74 , pp. 3597-3619
    • Moerner, W.E.1    Fromm, D.P.2
  • 42
    • 84875005538 scopus 로고    scopus 로고
    • Morrissey Lab Protocol for Preparing Phospholipid Vesicles (SUV) by Sonication
    • Accessed 2008
    • Morrissey Lab Protocol for Preparing Phospholipid Vesicles (SUV) by Sonication. Avanti Polar Lipids. http://avantilipids.com/images/PDF/ MorrisseyLabProtocolForPrepSuvBySonication.pdf. Accessed 2008.
    • Avanti Polar Lipids
  • 43
    • 0001215138 scopus 로고    scopus 로고
    • Formation and spreading of lipid bilayers on planar glass supports
    • P.S. Cremer, and S.G. Boxer Formation and spreading of lipid bilayers on planar glass supports J. Phys. Chem. 103 1999 2554 2559
    • (1999) J. Phys. Chem. , vol.103 , pp. 2554-2559
    • Cremer, P.S.1    Boxer, S.G.2
  • 44
    • 0017192686 scopus 로고
    • Mobility measurement by analysis of fluorescence photobleaching recovery kinetics
    • D. Axelrod, and D.E. Koppel W.W. Webb Mobility measurement by analysis of fluorescence photobleaching recovery kinetics Biophys. J. 16 1976 1055 1069
    • (1976) Biophys. J. , vol.16 , pp. 1055-1069
    • Axelrod, D.1    Koppel, D.E.2    Webb, W.W.3
  • 45
    • 0020568317 scopus 로고
    • Theoretical analysis of fluorescence photobleaching recovery experiments
    • D.M. Soumpasis Theoretical analysis of fluorescence photobleaching recovery experiments Biophys. J. 41 1983 95 97
    • (1983) Biophys. J. , vol.41 , pp. 95-97
    • Soumpasis, D.M.1
  • 46
    • 77950685282 scopus 로고    scopus 로고
    • Simultaneous single-molecule fluorescence and conductivity studies reveal distinct classes of Abeta species on lipid bilayers
    • J.A. Schauerte, and P.T. Wong A. Gafni Simultaneous single-molecule fluorescence and conductivity studies reveal distinct classes of Abeta species on lipid bilayers Biochemistry 49 2010 3031 3039
    • (2010) Biochemistry , vol.49 , pp. 3031-3039
    • Schauerte, J.A.1    Wong, P.T.2    Gafni, A.3
  • 47
    • 68949125204 scopus 로고    scopus 로고
    • Determination of the oligomer size of amyloidogenic protein β-amyloid(1-40) by single-molecule spectroscopy
    • H. Ding, and P.T. Wong D.G. Steel Determination of the oligomer size of amyloidogenic protein β-amyloid(1-40) by single-molecule spectroscopy Biophys. J. 97 2009 912 921
    • (2009) Biophys. J. , vol.97 , pp. 912-921
    • Ding, H.1    Wong, P.T.2    Steel, D.G.3
  • 48
    • 0032483035 scopus 로고    scopus 로고
    • Solution structure of amyloid beta-peptide(1-40) in a water-micelle environment. Is the membrane-spanning domain where we think it is?
    • M. Coles, and W. Bicknell D.J. Craik Solution structure of amyloid beta-peptide(1-40) in a water-micelle environment. Is the membrane-spanning domain where we think it is? Biochemistry 37 1998 11064 11077
    • (1998) Biochemistry , vol.37 , pp. 11064-11077
    • Coles, M.1    Bicknell, W.2    Craik, D.J.3
  • 49
    • 33846551354 scopus 로고    scopus 로고
    • Counting of six pRNAs of phi29 DNA-packaging motor with customized single-molecule dual-view system
    • D. Shu, and H. Zhang P. Guo Counting of six pRNAs of phi29 DNA-packaging motor with customized single-molecule dual-view system EMBO J. 26 2007 527 537
    • (2007) EMBO J. , vol.26 , pp. 527-537
    • Shu, D.1    Zhang, H.2    Guo, P.3
  • 50
    • 34247843089 scopus 로고    scopus 로고
    • Subunit counting in membrane-bound proteins
    • M.H. Ulbrich, and E.Y. Isacoff Subunit counting in membrane-bound proteins Nat. Methods 4 2007 319 321
    • (2007) Nat. Methods , vol.4 , pp. 319-321
    • Ulbrich, M.H.1    Isacoff, E.Y.2
  • 51
    • 0004653121 scopus 로고
    • Surface area per molecule in lipid/C12En membranes as seen by fluorescence resonance energy transfer
    • G. Lantzsch, H. Binder, and H. Heerklotz Surface area per molecule in lipid/C12En membranes as seen by fluorescence resonance energy transfer J. Fluoresc. 4 1994 339 343
    • (1994) J. Fluoresc. , vol.4 , pp. 339-343
    • Lantzsch, G.1    Binder, H.2    Heerklotz, H.3
  • 52
    • 0015855471 scopus 로고
    • Surface areas of naturally occurring lipid classes and the quantitative microdetermination of lipids
    • L.I. Burke, and G.S. Patil D.G. Cornwell Surface areas of naturally occurring lipid classes and the quantitative microdetermination of lipids J. Lipid Res. 14 1973 9 15
    • (1973) J. Lipid Res. , vol.14 , pp. 9-15
    • Burke, L.I.1    Patil, G.S.2    Cornwell, D.G.3
  • 53
    • 0043066616 scopus 로고    scopus 로고
    • Kinetics of adsorption of beta-amyloid peptide Abeta(1-40) to lipid bilayers
    • J.J. Kremer, and R.M. Murphy Kinetics of adsorption of beta-amyloid peptide Abeta(1-40) to lipid bilayers J. Biochem. Biophys. Methods 57 2003 159 169
    • (2003) J. Biochem. Biophys. Methods , vol.57 , pp. 159-169
    • Kremer, J.J.1    Murphy, R.M.2
  • 54
    • 0000291826 scopus 로고
    • Rates of diffusion controlled reactions in one, two and three dimensions
    • S.L. Hardt Rates of diffusion controlled reactions in one, two and three dimensions Biophys. Chem. 10 1979 239 243
    • (1979) Biophys. Chem. , vol.10 , pp. 239-243
    • Hardt, S.L.1
  • 55
    • 0021430791 scopus 로고
    • Relationship between lateral diffusion, collision frequency, and electron transfer of mitochondrial inner membrane oxidation-reduction components
    • S. Gupte, and E.S. Wu C.R. Hackenbrock Relationship between lateral diffusion, collision frequency, and electron transfer of mitochondrial inner membrane oxidation-reduction components Proc. Natl. Acad. Sci. USA 81 1984 2606 2610
    • (1984) Proc. Natl. Acad. Sci. USA , vol.81 , pp. 2606-2610
    • Gupte, S.1    Wu, E.S.2    Hackenbrock, C.R.3
  • 56
    • 80052059642 scopus 로고    scopus 로고
    • Direct observation of single amyloid-β(1-40) oligomers on live cells: Binding and growth at physiological concentrations
    • R.D. Johnson, and J.A. Schauerte D.G. Steel Direct observation of single amyloid-β(1-40) oligomers on live cells: binding and growth at physiological concentrations PLoS ONE 6 2011 e23970
    • (2011) PLoS ONE , vol.6 , pp. 23970
    • Johnson, R.D.1    Schauerte, J.A.2    Steel, D.G.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.