메뉴 건너뛰기




Volumn 1808, Issue 1, 2011, Pages 26-33

Effect of trehalose on the interaction of Alzheimer's Aβ-peptide and anionic lipid monolayers

Author keywords

Alzheimer's disease; Amyloid beta peptide; Membrane; Monolayer; Trehalose

Indexed keywords

AMYLOID BETA PROTEIN; LIPID; TREHALOSE;

EID: 78649790466     PISSN: 00052736     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbamem.2010.09.024     Document Type: Article
Times cited : (23)

References (70)
  • 1
    • 0031052381 scopus 로고    scopus 로고
    • Amyloid, the presenilins and Alzheimer's disease
    • J. Hardy Amyloid, the presenilins and Alzheimer's disease Trends Neurosci. 20 1997 154 159
    • (1997) Trends Neurosci. , vol.20 , pp. 154-159
    • Hardy, J.1
  • 2
    • 0028267440 scopus 로고
    • Normal and abnormal biology of the β-amyloid precursor protein
    • D.J. Selkoe Normal and abnormal biology of the β-amyloid precursor protein Annu. Rev. Neurosci. 17 1994 489 517
    • (1994) Annu. Rev. Neurosci. , vol.17 , pp. 489-517
    • Selkoe, D.J.1
  • 3
    • 0032556830 scopus 로고    scopus 로고
    • Alzheimer's disease: A technical KO of amyloid-bold beta peptide
    • C. Haas, and D.J. Selkoe Alzheimer's disease: a technical KO of amyloid-bold beta peptide Nature 391 1998 339 340
    • (1998) Nature , vol.391 , pp. 339-340
    • Haas, C.1    Selkoe, D.J.2
  • 4
    • 0346727128 scopus 로고    scopus 로고
    • Therapeutic approaches to protein-misfolding diseases
    • F.D. Cohen, and J.W. Kelly Therapeutic approaches to protein-misfolding diseases Nature 426 2003 905 909
    • (2003) Nature , vol.426 , pp. 905-909
    • Cohen, F.D.1    Kelly, J.W.2
  • 5
    • 0032084472 scopus 로고    scopus 로고
    • Structural and kinetic features of amyloid beta-protein fibrillogenesis
    • D.B. Teplow Structural and kinetic features of amyloid beta-protein fibrillogenesis Amyloid 5 1998
    • (1998) Amyloid , vol.5
    • Teplow, D.B.1
  • 6
    • 0030799122 scopus 로고    scopus 로고
    • Amyloid beta-protein fibrillogenesis - Detection of a protofibrillar intermediate
    • D.M. Walsh, A. Lomakin, G.B. Benedek, M.M. Condron, and D.B. Teplow Amyloid beta-protein fibrillogenesis - detection of a protofibrillar intermediate J. Biol. Chem. 272 1997 22364 22372
    • (1997) J. Biol. Chem. , vol.272 , pp. 22364-22372
    • Walsh, D.M.1    Lomakin, A.2    Benedek, G.B.3    Condron, M.M.4    Teplow, D.B.5
  • 7
    • 33646557678 scopus 로고    scopus 로고
    • The role of lipid-protein interactions in amyloid-type protein fibril formation
    • G.P. Gorbenko, and P.K.J. Kinnunen The role of lipid-protein interactions in amyloid-type protein fibril formation Chem. Phys. Lipids 141 2006 72 82
    • (2006) Chem. Phys. Lipids , vol.141 , pp. 72-82
    • Gorbenko, G.P.1    Kinnunen, P.K.J.2
  • 8
    • 0033863798 scopus 로고    scopus 로고
    • Review: Modulating factors in amyloid-β fibril formation
    • J. McLaurin, D.S. Yang, C.M. Yip, and P.E. Fraser Review: modulating factors in amyloid-β fibril formation J. Struct. Biol. 130 2000 259 270
    • (2000) J. Struct. Biol. , vol.130 , pp. 259-270
    • McLaurin, J.1    Yang, D.S.2    Yip, C.M.3    Fraser, P.E.4
  • 9
    • 0028982292 scopus 로고
    • Self-association of β-amyloid peptide (1-40) in solution and binding to lipid membranes
    • E. Terzi, G. Hölzemann, and J. Seelig Self-association of β-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
  • 10
    • 0342378042 scopus 로고    scopus 로고
    • Interaction of Alzheimer β-amyloid peptide (1-40) with lipid membranes
    • E. Terzi, G. Hölzemann, and J. Seelig Interaction of Alzheimer β-amyloid peptide (1-40) with lipid membranes Biochemistry 36 1997 14845 14852
    • (1997) Biochemistry , vol.36 , pp. 14845-14852
    • Terzi, E.1    Hölzemann, G.2    Seelig, J.3
  • 11
    • 0034663858 scopus 로고    scopus 로고
    • Accelerated accumulation of amyloid β proteins on oxidatively damaged lipid membranes
    • V. Koppaka, and P.H. Axelsen Accelerated accumulation of amyloid β proteins on oxidatively damaged lipid membranes Biochemistry 36 2000 10011 10016
    • (2000) Biochemistry , vol.36 , pp. 10011-10016
    • Koppaka, V.1    Axelsen, P.H.2
  • 12
    • 0030892291 scopus 로고    scopus 로고
    • Characterization of the interactions of Alzheimer β-Amyloid peptides with phospholipid membranes
    • J.A. McLaurin, and A. Chakrabbartty Characterization of the interactions of Alzheimer β-Amyloid peptides with phospholipid membranes Eur. J. Biochem. 245 1997 355 363
    • (1997) Eur. J. Biochem. , vol.245 , pp. 355-363
    • McLaurin, J.A.1    Chakrabbartty, A.2
  • 13
    • 77953235479 scopus 로고    scopus 로고
    • A beta polymerization through interaction with membrane gangliosides
    • K. Matsuzaki, K. Kato, and K. Yanagisawa A beta polymerization through interaction with membrane gangliosides BBA Mol. Cell. Biol. L. 1801 2010 868 877
    • (2010) BBA Mol. Cell. Biol. L. , vol.1801 , pp. 868-877
    • Matsuzaki, K.1    Kato, K.2    Yanagisawa, K.3
  • 14
    • 33846703726 scopus 로고    scopus 로고
    • Adsorption of amyloid β (1-40) peptide at liquid interfaces
    • G. Brezesinski, E. Maltseva, and H. Möhwald Adsorption of amyloid β (1-40) peptide at liquid interfaces J. Phys. Chem. 221 2007 95 111
    • (2007) J. Phys. Chem. , vol.221 , pp. 95-111
    • Brezesinski, G.1    Maltseva, E.2    Möhwald, H.3
  • 15
    • 0344823652 scopus 로고    scopus 로고
    • Externally administered amyloid β peptide 25-35 and perturbation of lipid bilayers
    • S. Dante, T. Hauß, A. Brandt, and N.A. Dencher Externally administered amyloid β peptide 25-35 and perturbation of lipid bilayers Biochemistry 42 2003 13667 13672
    • (2003) Biochemistry , vol.42 , pp. 13667-13672
    • Dante, S.1    Hauß, T.2    Brandt, A.3    Dencher, N.A.4
  • 16
    • 0035159553 scopus 로고    scopus 로고
    • Amyloid β protein forms ion channels: Implications for Alzheimer's disease pathology
    • H. Lin, L. Bhatia, and R. Lal Amyloid β protein forms ion channels: implications for Alzheimer's disease pathology FASEB J. 15 2001 2433 2444
    • (2001) FASEB J. , vol.15 , pp. 2433-2444
    • Lin, H.1    Bhatia, L.2    Lal, R.3
  • 18
    • 70350196379 scopus 로고    scopus 로고
    • Surface chemistry of Alzheimer's disease: A Langmuir monolayer approach
    • G. Thakur, M. Micic, and R.M. Leblanc Surface chemistry of Alzheimer's disease: a Langmuir monolayer approach Colloid Surf. B 74 2009 436 456
    • (2009) Colloid Surf. B , vol.74 , pp. 436-456
    • Thakur, G.1    Micic, M.2    Leblanc, R.M.3
  • 19
    • 0037551741 scopus 로고    scopus 로고
    • Protofibrils, pores, fibrils, and neurodegeneration: Separating the responsible protein aggregates from the innocent bystanders
    • C. Caughey, and P.T. Lansbury Protofibrils, pores, fibrils, and neurodegeneration: separating the responsible protein aggregates from the innocent bystanders Annu. Rev. Neurosci. 26 2003 267 298
    • (2003) Annu. Rev. Neurosci. , vol.26 , pp. 267-298
    • Caughey, C.1    Lansbury, P.T.2
  • 20
    • 0000977345 scopus 로고    scopus 로고
    • Channel formation in the pathogenesis of Alzheimer's disease and other amyloidoses
    • Y. Hirakura, and B.L. Kegan Channel formation in the pathogenesis of Alzheimer's disease and other amyloidoses Einstein Q. J. Biol. Med. 16 1999 124 129
    • (1999) Einstein Q. J. Biol. Med. , vol.16 , pp. 124-129
    • Hirakura, Y.1    Kegan, B.L.2
  • 21
    • 85081450888 scopus 로고    scopus 로고
    • Alzheimer's amyloid β-protein forms Ca2+-permeable channels in neuronal cells and its aggregation is stimulated by aluminum
    • M. Kawahara, and Y. Kuroda Alzheimer's amyloid β-protein forms Ca2+-permeable channels in neuronal cells and its aggregation is stimulated by aluminum J. Neurochem. 69 1997 S46
    • (1997) J. Neurochem. , vol.69 , pp. 46
    • Kawahara, M.1    Kuroda, Y.2
  • 22
    • 0033600590 scopus 로고    scopus 로고
    • Amyloid β protein (1-40) forms calcium-permeable, Zn2+-sensitive channel in reconstituted lipid vesicles
    • H. Lin, Y.W.J. Zhu, and R. Lal Amyloid β protein (1-40) forms calcium-permeable, Zn2+-sensitive channel in reconstituted lipid vesicles Biochemistry 38 1999 11189 11196
    • (1999) Biochemistry , vol.38 , pp. 11189-11196
    • Lin, H.1    Zhu, Y.W.J.2    Lal, R.3
  • 24
    • 4444328762 scopus 로고    scopus 로고
    • Insertion of Alzheimer's Aβ40 peptide into lipid monolayers
    • C. Ege, and K.Y.C. Lee Insertion of Alzheimer's Aβ40 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
  • 25
    • 27944467440 scopus 로고    scopus 로고
    • Nonfibrous β-structured aggregation of an Aβ model peptide (Ad-1α) on GM1/DPPC mixed monolayer surfaces
    • T. Kawasaki, K. Asaoka, H. Mihara, and Y. Okhata Nonfibrous β-structured aggregation of an Aβ model peptide (Ad-1α) on GM1/DPPC mixed monolayer surfaces J. Colloid Interface Sci. 294 2006 295 303
    • (2006) J. Colloid Interface Sci. , vol.294 , pp. 295-303
    • Kawasaki, T.1    Asaoka, K.2    Mihara, H.3    Okhata, Y.4
  • 26
    • 26944494925 scopus 로고    scopus 로고
    • Adsorption of amyloid β (1-40) peptide at phospholipid monolayers
    • E. Maltseva, A. Kerth, A. Blume, H. Möhwald, and G. Brezesinski Adsorption of amyloid β (1-40) peptide at phospholipid monolayers Chembiochem 6 2005 1817 1824
    • (2005) Chembiochem , vol.6 , pp. 1817-1824
    • Maltseva, E.1    Kerth, A.2    Blume, A.3    Möhwald, H.4    Brezesinski, G.5
  • 27
    • 44949154514 scopus 로고    scopus 로고
    • Lipid membrane templates the ordering and induces the fibrillogenesis of Alzheimer's disease amyloid-β peptide
    • E.Y. Chi, A. Winans, J. Majewski, G. Wu, K. Kjaer, and K.Y.C. Lee Lipid membrane templates the ordering and induces the fibrillogenesis of Alzheimer's disease amyloid-β peptide Proteins 72 2008 1 24
    • (2008) Proteins , vol.72 , pp. 1-24
    • Chi, E.Y.1    Winans, A.2    Majewski, J.3    Wu, G.4    Kjaer, K.5    Lee, K.Y.C.6
  • 29
    • 2442483898 scopus 로고    scopus 로고
    • Peripheral treatment with enoxaparin, a low molecular weight heparin, reduces plaques and β-amyloid accumulation in a mouse model of Alzheimer's disease
    • L. Bergamaschini, E. Rossi, C. Storini, S. Pizzimenti, M. Distaso, C. Perego, A. De Luigi, C. Vergani, and M.G. De Simoni Peripheral treatment with enoxaparin, a low molecular weight heparin, reduces plaques and β-amyloid accumulation in a mouse model of Alzheimer's disease J. Neurosci. 24 2004 4181 4186
    • (2004) J. Neurosci. , vol.24 , pp. 4181-4186
    • Bergamaschini, L.1    Rossi, E.2    Storini, C.3    Pizzimenti, S.4    Distaso, M.5    Perego, C.6    De Luigi, A.7    Vergani, C.8    De Simoni, M.G.9
  • 30
    • 4344650564 scopus 로고    scopus 로고
    • Dopamine and L-dopa disaggregate amyloid fibrils: Implications for Parkinson's and Alzheimer's disease
    • J. Li, M. Zhu, A.B. Manning-Bog, D.A. Di Monte, and A.L. Fink Dopamine and L-dopa disaggregate amyloid fibrils: implications for Parkinson's and Alzheimer's disease FASEB J. 18 2004 962 964
    • (2004) FASEB J. , vol.18 , pp. 962-964
    • Li, J.1    Zhu, M.2    Manning-Bog, A.B.3    Di Monte, D.A.4    Fink, A.L.5
  • 32
    • 1542364225 scopus 로고    scopus 로고
    • Curcumin has potent anti-amyloidogenic effects for Alzheimer's β-amyloid fibrils in vitro
    • K. Ono, K. Hasegawa, H. Nakiki, and M. Yamada Curcumin has potent anti-amyloidogenic effects for Alzheimer's β-amyloid fibrils in vitro J. Neurosci. Res. 75 2004 742 750
    • (2004) J. Neurosci. Res. , vol.75 , pp. 742-750
    • Ono, K.1    Hasegawa, K.2    Nakiki, H.3    Yamada, M.4
  • 33
    • 0032539975 scopus 로고    scopus 로고
    • Oligomerization of endogenous and synthetic amyloid β-protein at nanomolar levels in cell culture and stabilization of monomer by Congo red
    • M.B. Podlisny, D.M. Walsh, P. Amarante, B.L. Ostazewski, E.R. Stimson, J.E. Maggio, D.B. Teplow, and D.J. Selkoe Oligomerization of endogenous and synthetic amyloid β-protein at nanomolar levels in cell culture and stabilization of monomer by Congo red Biochemistry 37 1998 3602 3611
    • (1998) Biochemistry , vol.37 , pp. 3602-3611
    • Podlisny, M.B.1    Walsh, D.M.2    Amarante, P.3    Ostazewski, B.L.4    Stimson, E.R.5    Maggio, J.E.6    Teplow, D.B.7    Selkoe, D.J.8
  • 35
    • 24044483249 scopus 로고    scopus 로고
    • Trehalose differentially inhibits aggregation and neurotoxicity of β-amyloid 40 and 42
    • R. Liu, H. Barkhordarian, S. Emadi, C.B. Park, and M.R. Sierks Trehalose differentially inhibits aggregation and neurotoxicity of β-amyloid 40 and 42 Neurobiol. Dis. 20 2005 74 81
    • (2005) Neurobiol. Dis. , vol.20 , pp. 74-81
    • Liu, R.1    Barkhordarian, H.2    Emadi, S.3    Park, C.B.4    Sierks, M.R.5
  • 36
    • 48449085158 scopus 로고    scopus 로고
    • Inhibition of Alzheimer amyloid β aggregation by polyvalent trehalose
    • Y. Miura, C. You, and R. Ohnishi Inhibition of Alzheimer amyloid β aggregation by polyvalent trehalose Sci. Technol. Adv. Mat. 9 2008 24407 24412
    • (2008) Sci. Technol. Adv. Mat. , vol.9 , pp. 24407-24412
    • Miura, Y.1    You, C.2    Ohnishi, R.3
  • 37
    • 1842850631 scopus 로고    scopus 로고
    • Inhibition of insulin amyloid formation by small stress molecules
    • A. Arora, C. Ha, and C.B. Park Inhibition of insulin amyloid formation by small stress molecules FEBS Lett. 564 2004 121 125
    • (2004) FEBS Lett. , vol.564 , pp. 121-125
    • Arora, A.1    Ha, C.2    Park, C.B.3
  • 39
    • 30544440028 scopus 로고    scopus 로고
    • Modulating membrane properties: The effect of trehalose and cholesterol on a phospholipid bilayer
    • M. Doxastakis, A.K. Sum, and J.J. de Pablo Modulating membrane properties: the effect of trehalose and cholesterol on a phospholipid bilayer J. Phys. Chem. B 109 2005 24173 24181
    • (2005) J. Phys. Chem. B , vol.109 , pp. 24173-24181
    • Doxastakis, M.1    Sum, A.K.2    De Pablo, J.J.3
  • 40
    • 20644470101 scopus 로고    scopus 로고
    • Phase behavior of freeze-dried phospholipid-cholesterol mixtures stabilized with trehalose
    • S. Ohtake, C. Schebor, S.P. Palecek, and J.J. de Pablo Phase behavior of freeze-dried phospholipid-cholesterol mixtures stabilized with trehalose BBA Biomembr. 1713 2005 57 64
    • (2005) BBA Biomembr. , vol.1713 , pp. 57-64
    • Ohtake, S.1    Schebor, C.2    Palecek, S.P.3    De Pablo, J.J.4
  • 42
    • 69549086151 scopus 로고    scopus 로고
    • Effect of trehalose on amyloid β (29-40)-membrane interaction
    • A.S. Reddy, A. Izmitli, and J.J. de Pablo Effect of trehalose on amyloid β (29-40)-membrane interaction J. Phys. Chem. 131 2009 085101/1-8
    • (2009) J. Phys. Chem. , vol.131
    • Reddy, A.S.1    Izmitli, A.2    De Pablo, J.J.3
  • 43
    • 0018795945 scopus 로고
    • A comparative study of the phase transitions of phospholipid bilayers and monolayers
    • A. Blume A comparative study of the phase transitions of phospholipid bilayers and monolayers Biochim. Biophys. Acta 557 1979 32 44
    • (1979) Biochim. Biophys. Acta , vol.557 , pp. 32-44
    • Blume, A.1
  • 44
    • 0031983218 scopus 로고    scopus 로고
    • Solvation effects of dimethyl sulphoxide on the structure of phospholipid bilayers
    • Z.W. Yu, and P.J. Quinn Solvation effects of dimethyl sulphoxide on the structure of phospholipid bilayers Biophys. J. 70 1998 35 39
    • (1998) Biophys. J. , vol.70 , pp. 35-39
    • Yu, Z.W.1    Quinn, P.J.2
  • 45
    • 0345413296 scopus 로고    scopus 로고
    • Molecular simulation study on the influence of dimethylsulfoxide on the structure of phospholipid bilayers
    • A.K. Sum, and J.J. de Pablo Molecular simulation study on the influence of dimethylsulfoxide on the structure of phospholipid bilayers Biophys. J. 85 2003 3636 3645
    • (2003) Biophys. J. , vol.85 , pp. 3636-3645
    • Sum, A.K.1    De Pablo, J.J.2
  • 46
    • 57049174009 scopus 로고    scopus 로고
    • Structures of rat and human islet amyloid polypeptide IAPP1-19 in micelles by NMR spectroscopy
    • R.P.R. Nanga, J.R. Brender, J. Xu, G. Veglia, and A. Ramamoorthy Structures of rat and human islet amyloid polypeptide IAPP1-19 in micelles by NMR spectroscopy Biochemistry 47 2008 12689 12697
    • (2008) Biochemistry , vol.47 , pp. 12689-12697
    • Nanga, R.P.R.1    Brender, J.R.2    Xu, J.3    Veglia, G.4    Ramamoorthy, A.5
  • 47
    • 71749085062 scopus 로고    scopus 로고
    • Structures of beta-amyloid peptide 1-40, 1-42, and 1-55 - The 672-726 fragment of APP - In a membrane environment with implications for interactions with gamma-secretase
    • N. Miyashita, J.E. Straub, and D. Thirumalai Structures of beta-amyloid peptide 1-40, 1-42, and 1-55 - the 672-726 fragment of APP - in a membrane environment with implications for interactions with gamma-secretase J. Am. Chem. Soc. 131 2009 17843 17852
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 17843-17852
    • Miyashita, N.1    Straub, J.E.2    Thirumalai, D.3
  • 48
    • 65549152828 scopus 로고    scopus 로고
    • Perturbation of membranes by amyloid β peptide - A molecular dynamics study
    • J.A. Lemkul, and D.R. Revan Perturbation of membranes by amyloid β peptide - a molecular dynamics study FEBS J. 276 2009 3060 3075
    • (2009) FEBS J. , vol.276 , pp. 3060-3075
    • Lemkul, J.A.1    Revan, D.R.2
  • 49
    • 0242385390 scopus 로고    scopus 로고
    • Molecular simulation study of phospholipid bilayers and insights of the interactions with disaccharides
    • A.K. Sum, R. Faller, and J.J. de Pablo Molecular simulation study of phospholipid bilayers and insights of the interactions with disaccharides Biophys. J. 85 2003 2830 2844
    • (2003) Biophys. J. , vol.85 , pp. 2830-2844
    • Sum, A.K.1    Faller, R.2    De Pablo, J.J.3
  • 50
    • 33947139278 scopus 로고    scopus 로고
    • Setting up and running molecular dynamics simulations of membrane proteins
    • C. Kandt, W.L. Ash, and D.P. Tieleman Setting up and running molecular dynamics simulations of membrane proteins Methods 41 2007 475 488
    • (2007) Methods , vol.41 , pp. 475-488
    • Kandt, C.1    Ash, W.L.2    Tieleman, D.P.3
  • 54
    • 85081442505 scopus 로고    scopus 로고
    • CD and NMR studies of aggregation of amyloid-β(1-40) peptide upon binding to model and raft membranes
    • M. Bokvist, F. Lindstrom, and G. Grobner CD and NMR studies of aggregation of amyloid-β(1-40) peptide upon binding to model and raft membranes Biophys. J. 84 2003 56A
    • (2003) Biophys. J. , vol.84
    • Bokvist, M.1    Lindstrom, F.2    Grobner, G.3
  • 55
    • 0037155235 scopus 로고    scopus 로고
    • Cholesterol is an important factor affecting the membrane insertion of β-Amyloid peptide (Aβ1-40), which may potentially inhibit the fibril formation
    • S.-R. Ji, Y. Wu, and S.-F. Sui Cholesterol is an important factor affecting the membrane insertion of β-Amyloid peptide (Aβ1-40), which may potentially inhibit the fibril formation J. Biol. Chem. 277 2002 6273 6279
    • (2002) J. Biol. Chem. , vol.277 , pp. 6273-6279
    • Ji, S.-R.1    Wu, Y.2    Sui, S.-F.3
  • 56
    • 0032483035 scopus 로고    scopus 로고
    • Solution structure of amyloid β-peptide (1-40) in a water-micelle environment. Is the membrane-spanning domain where we think it is?
    • M. Coles, W. Bicknell, A.A. Watson, D.P. Fairlie, and D.J. Craik Solution structure of amyloid β-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    Watson, A.A.3    Fairlie, D.P.4    Craik, D.J.5
  • 57
    • 0037474240 scopus 로고    scopus 로고
    • Metal ions, pH, and cholesterol regulate the interactions of Alzheimer's disease amyloid-β peptide with membrane lipid
    • C.C. Curtain, F.E. Ali, D.G. Smith, A.I. Bush, C.L. Masters, and K.J. Barnham Metal ions, pH, and cholesterol regulate the interactions of Alzheimer's disease amyloid-β peptide with membrane lipid J. Biol. Chem. 278 2003 2977 2982
    • (2003) J. Biol. Chem. , vol.278 , pp. 2977-2982
    • Curtain, C.C.1    Ali, F.E.2    Smith, D.G.3    Bush, A.I.4    Masters, C.L.5    Barnham, K.J.6
  • 59
    • 70149116768 scopus 로고    scopus 로고
    • Association of highly compact type II diabetes related islet amyloid polypeptide intermediate species at physiological temperature revealed by diffusion NMR spectroscopy
    • R. Soong, J.R. Brender, P.M. Macdonald, and A. Ramamoorthy Association of highly compact type II diabetes related islet amyloid polypeptide intermediate species at physiological temperature revealed by diffusion NMR spectroscopy J. Am. Chem. Soc. 131 2009 7079 7085
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 7079-7085
    • Soong, R.1    Brender, J.R.2    MacDonald, P.M.3    Ramamoorthy, A.4
  • 62
    • 0032483735 scopus 로고    scopus 로고
    • Solution structure model of residues 1-28 of the amyloid beta peptide when bound to micelles
    • K.J. Marcinowski, H. Shao, E.L. Clancy, and M.G. Zagorski Solution structure model of residues 1-28 of the amyloid beta peptide when bound to micelles J. Am. Chem. Soc. 120 1998 11082 11091
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 11082-11091
    • Marcinowski, K.J.1    Shao, H.2    Clancy, E.L.3    Zagorski, M.G.4
  • 63
    • 0033555275 scopus 로고    scopus 로고
    • Solution structures of micelle bound amyloid beta (1-40) and beta (1-42) peptides of Alzheimers's disease
    • H.Y. Shao, S.C. Jao, K. Ma, and M.G. Zagorski Solution structures of micelle bound amyloid beta (1-40) and beta (1-42) peptides of Alzheimers's disease J. Mol. Biol. 285 1999 755 773
    • (1999) J. Mol. Biol. , vol.285 , pp. 755-773
    • Shao, H.Y.1    Jao, S.C.2    Ma, K.3    Zagorski, M.G.4
  • 65
    • 0030040794 scopus 로고    scopus 로고
    • On the role of surface tension in the stabilization of globular proteins
    • T.Y. Lin, and S.N. Timasheff On the role of surface tension in the stabilization of globular proteins Protein Sci. 5 1996 372 381
    • (1996) Protein Sci. , vol.5 , pp. 372-381
    • Lin, T.Y.1    Timasheff, S.N.2
  • 66
    • 0035282963 scopus 로고    scopus 로고
    • Cutinase unfolding and stabilization by trehalose and mannosylglycerate
    • E.P. Melo, T.Q. Faria, L.O. Martins, A.M.G.c. Calves, and J.M.S. Cabral Cutinase unfolding and stabilization by trehalose and mannosylglycerate Proteins 42 2001 542 552
    • (2001) Proteins , vol.42 , pp. 542-552
    • Melo, E.P.1    Faria, T.Q.2    Martins, L.O.3    A, C.G.M.C.4    Cabral, J.M.S.5
  • 67
    • 0030973690 scopus 로고    scopus 로고
    • The thermodynamic mechanism of protein stabilization
    • G. Xie, and S.N. Timasheff The thermodynamic mechanism of protein stabilization Biophys. Chem. 64 1997 25 43
    • (1997) Biophys. Chem. , vol.64 , pp. 25-43
    • Xie, G.1    Timasheff, S.N.2
  • 68
  • 69
    • 28444481767 scopus 로고    scopus 로고
    • A molecular dynamics study of the response of lipid bilayers and monolayers on trehalose
    • A. Skibinsky, R.M. Venable, and R.W. Pastor A molecular dynamics study of the response of lipid bilayers and monolayers on trehalose Biophys. J. 89 2005 4111 4121
    • (2005) Biophys. J. , vol.89 , pp. 4111-4121
    • Skibinsky, A.1    Venable, R.M.2    Pastor, R.W.3
  • 70
    • 0029619259 scopus 로고
    • Knowledge-based secondary structure assignment
    • D. Frishman, and P. Argos Knowledge-based secondary structure assignment Proteins 23 1995 566 579
    • (1995) Proteins , vol.23 , pp. 566-579
    • Frishman, D.1    Argos, P.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.