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Volumn 1798, Issue 3, 2010, Pages 660-671

Membrane charge dependent states of the β-amyloid fragment Aβ (16-35) with differently charged micelle aggregates

Author keywords

Amyloid peptide; EPR spectroscopy; Micelle solution; NMR spectroscopy; Spin labeled peptide

Indexed keywords

AMPHOLYTE; AMYLOID BETA PROTEIN; AMYLOID BETA PROTEIN(16-35); METHYL 3 (2,2,5,5 TETRAMETHYL 1 OXYPYRROLINYL)METHANETHIOLSULFONATE; UNCLASSIFIED DRUG;

EID: 76749118593     PISSN: 00052736     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbamem.2009.12.012     Document Type: Article
Times cited : (26)

References (95)
  • 1
    • 0035066332 scopus 로고    scopus 로고
    • Alzheimer's disease: genes, proteins, and therapy
    • Selkoe D.J. Alzheimer's disease: genes, proteins, and therapy. Physiol. Rev. 81 (2001) 741-766
    • (2001) Physiol. Rev. , vol.81 , pp. 741-766
    • Selkoe, D.J.1
  • 2
    • 5344277556 scopus 로고    scopus 로고
    • Deciphering the molecular basis of memory failure in Alzheimer's disease
    • Walsh D.M., and Selkoe D.J. Deciphering the molecular basis of memory failure in Alzheimer's disease. Neuron 44 (2004) 181-193
    • (2004) Neuron , vol.44 , pp. 181-193
    • Walsh, D.M.1    Selkoe, D.J.2
  • 3
    • 0033849738 scopus 로고    scopus 로고
    • Review: history of the amyloid fibril
    • Sipe J.D., and Cohen A.S. Review: history of the amyloid fibril. J. Struct. Biol. 130 (2000) 88-98
    • (2000) J. Struct. Biol. , vol.130 , pp. 88-98
    • Sipe, J.D.1    Cohen, A.S.2
  • 4
    • 0037135111 scopus 로고    scopus 로고
    • The amyloid hypothesis of Alzheimer's disease: progress and problems on the road to therapeutics
    • Hardy J., and Selkoe D.J. The amyloid hypothesis of Alzheimer's disease: progress and problems on the road to therapeutics. Science 297 (2002) 353-356
    • (2002) Science , vol.297 , pp. 353-356
    • Hardy, J.1    Selkoe, D.J.2
  • 5
    • 43549100675 scopus 로고    scopus 로고
    • Islet amyloid in type 2 diabetes, and the toxic oligomer hypothesis
    • Haataja L., Gurlo T., Huang C.J., and Butler P.C. Islet amyloid in type 2 diabetes, and the toxic oligomer hypothesis. Endocr. Rev. 29 (2008) 303-316
    • (2008) Endocr. Rev. , vol.29 , pp. 303-316
    • Haataja, L.1    Gurlo, T.2    Huang, C.J.3    Butler, P.C.4
  • 6
    • 0037415751 scopus 로고    scopus 로고
    • From Alzheimer to Huntington: why is a structural understanding so difficult?
    • Temussi P.A., Masino L., and Pastore A. From Alzheimer to Huntington: why is a structural understanding so difficult?. EMBO J. 22 (2003) 355-361
    • (2003) EMBO J. , vol.22 , pp. 355-361
    • Temussi, P.A.1    Masino, L.2    Pastore, A.3
  • 7
    • 0033600274 scopus 로고    scopus 로고
    • Translating cell biology into therapeutic advances in Alzheimer's disease
    • Selkoe D.J. Translating cell biology into therapeutic advances in Alzheimer's disease. Nature 399 (1999) A23-A31
    • (1999) Nature , vol.399
    • Selkoe, D.J.1
  • 9
    • 0022547855 scopus 로고
    • X-ray diffraction from intraneuronal paired helical filaments and extraneuronal amyloid fibers in Alzheimer disease indicates cross-beta conformation
    • Kirschner D.A., Abraham C., and Selkoe D.J. X-ray diffraction from intraneuronal paired helical filaments and extraneuronal amyloid fibers in Alzheimer disease indicates cross-beta conformation. Proc. Natl. Acad. Sci. U. S. A. 83 (1986) 503-507
    • (1986) Proc. Natl. Acad. Sci. U. S. A. , vol.83 , pp. 503-507
    • Kirschner, D.A.1    Abraham, C.2    Selkoe, D.J.3
  • 10
    • 0028980362 scopus 로고
    • The alpha-helical to beta-strand transition in the amino-terminal fragment of the amyloid beta-peptide modulates amyloid formation
    • Soto C., Castano E.M., Frangione B., and Inestrosa N.C. The alpha-helical to beta-strand transition in the amino-terminal fragment of the amyloid beta-peptide modulates amyloid formation. J. Biol. Chem. 270 (1995) 3063-3067
    • (1995) J. Biol. Chem. , vol.270 , pp. 3063-3067
    • Soto, C.1    Castano, E.M.2    Frangione, B.3    Inestrosa, N.C.4
  • 11
    • 0033863798 scopus 로고    scopus 로고
    • Review: modulating factors in amyloid-beta fibril formation
    • McLaurin J., Yang D., Yip C.M., and Fraser P.E. Review: modulating factors in amyloid-beta fibril formation. J. Struct. Biol. 130 (2000) 259-270
    • (2000) J. Struct. Biol. , vol.130 , pp. 259-270
    • McLaurin, J.1    Yang, D.2    Yip, C.M.3    Fraser, P.E.4
  • 13
    • 0031873102 scopus 로고    scopus 로고
    • Beta-sheet breaker peptides inhibit fibrillogenesis in a rat brain model of amyloidosis: implications for Alzheimer's therapy
    • Soto C., Sigurdsson E.M., Morelli L., Kumar R.A., Castano E.M., and Frangione B. Beta-sheet breaker peptides inhibit fibrillogenesis in a rat brain model of amyloidosis: implications for Alzheimer's therapy. Nat. Med. 4 (1998) 822-826
    • (1998) Nat. Med. , vol.4 , pp. 822-826
    • Soto, C.1    Sigurdsson, E.M.2    Morelli, L.3    Kumar, R.A.4    Castano, E.M.5    Frangione, B.6
  • 16
    • 42449111198 scopus 로고    scopus 로고
    • Stabilization of a -hairpin in monomeric Alzheimer's amyloid- peptide inhibits amyloid formation
    • Hoyer W., Grönwall C., Jonsson A., Ståhl S., and Härd T. Stabilization of a -hairpin in monomeric Alzheimer's amyloid- peptide inhibits amyloid formation. Proc. Natl. Acad. Sci. 105 (2008) 5099
    • (2008) Proc. Natl. Acad. Sci. , vol.105 , pp. 5099
    • Hoyer, W.1    Grönwall, C.2    Jonsson, A.3    Ståhl, S.4    Härd, T.5
  • 17
    • 33646557678 scopus 로고    scopus 로고
    • The role of lipid-protein interactions in amyloid-type protein fibril formation
    • Gorbenko G.P., and Kinnunen P.K. 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.2
  • 18
    • 11144221004 scopus 로고    scopus 로고
    • Amyloid accomplices and enforcers
    • Alexandrescu A.T. Amyloid accomplices and enforcers. Protein Sci. 14 (2005) 1-12
    • (2005) Protein Sci. , vol.14 , pp. 1-12
    • Alexandrescu, A.T.1
  • 19
    • 0030908095 scopus 로고    scopus 로고
    • Models of amyloid seeding in Alzheimer's disease and scrapie: mechanistic truths and physiological consequences of the time-dependent solubility of amyloid proteins
    • Harper J.D., and Lansbury Jr. P.T. Models of amyloid seeding in Alzheimer's disease and scrapie: mechanistic truths and physiological consequences of the time-dependent solubility of amyloid proteins. Annu. Rev. Biochem. 66 (1997) 385-407
    • (1997) Annu. Rev. Biochem. , vol.66 , pp. 385-407
    • Harper, J.D.1    Lansbury Jr., P.T.2
  • 20
    • 22244439242 scopus 로고    scopus 로고
    • The aggregation kinetics of Alzheimer's beta-amyloid peptide is controlled by stochastic nucleation
    • Hortschansky P., Schroeckh V., Christopeit T., Zandomeneghi G., and Fandrich M. The aggregation kinetics of Alzheimer's beta-amyloid peptide is controlled by stochastic nucleation. Protein Sci. 14 (2005) 1753-1759
    • (2005) Protein Sci. , vol.14 , pp. 1753-1759
    • Hortschansky, P.1    Schroeckh, V.2    Christopeit, T.3    Zandomeneghi, G.4    Fandrich, M.5
  • 21
    • 67650533782 scopus 로고    scopus 로고
    • Three-dimensional structure and orientation of rat islet amyloid polypeptide protein in a membrane environment by solution NMR spectroscopy
    • Nanga R., Brender J., Xu J., Hartman K., Subramanian V., and Ramamoorthy A. Three-dimensional structure and orientation of rat islet amyloid polypeptide protein in a membrane environment by solution NMR spectroscopy. J. Am. Chem. Soc. 131 (2009) 8252-8261
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 8252-8261
    • Nanga, R.1    Brender, J.2    Xu, J.3    Hartman, K.4    Subramanian, V.5    Ramamoorthy, A.6
  • 22
    • 33847662852 scopus 로고    scopus 로고
    • Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer's amyloid beta-peptide
    • Haass C., and Selkoe D.J. Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer's amyloid beta-peptide. Nat. Rev. Mol. Cell. Biol. 8 (2007) 101-112
    • (2007) Nat. Rev. Mol. Cell. Biol. , vol.8 , pp. 101-112
    • Haass, C.1    Selkoe, D.J.2
  • 23
    • 43949107500 scopus 로고    scopus 로고
    • Amyloid fiber formation and membrane disruption are separate processes localized in two distinct regions of IAPP, the type-2-diabetes-related peptide
    • Brender J., Lee E., Cavitt M., Gafni A., Steel D., and Ramamoorthy A. Amyloid fiber formation and membrane disruption are separate processes localized in two distinct regions of IAPP, the type-2-diabetes-related peptide. J. Am. Chem. Soc. 130 (2008) 6424-6429
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 6424-6429
    • Brender, J.1    Lee, E.2    Cavitt, M.3    Gafni, A.4    Steel, D.5    Ramamoorthy, A.6
  • 24
    • 57049174009 scopus 로고    scopus 로고
    • Structures of rat and human islet amyloid polypeptide IAPP1-19 in micelles by NMR spectroscopy†
    • Nanga R., Brender J., Xu J., Veglia G., and Ramamoorthy A. 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.1    Brender, J.2    Xu, J.3    Veglia, G.4    Ramamoorthy, A.5
  • 25
    • 57049086457 scopus 로고    scopus 로고
    • A single mutation in the nonamyloidogenic region of islet amyloid polypeptide greatly reduces toxicity†
    • Brender J., Hartman K., Reid K., Kennedy R., and Ramamoorthy A. A single mutation in the nonamyloidogenic region of islet amyloid polypeptide greatly reduces toxicity†. Biochemistry 47 (2008) 12680-12688
    • (2008) Biochemistry , vol.47 , pp. 12680-12688
    • Brender, J.1    Hartman, K.2    Reid, K.3    Kennedy, R.4    Ramamoorthy, A.5
  • 26
    • 0036830947 scopus 로고    scopus 로고
    • Calcium dyshomeostasis and intracellular signalling in Alzheimer's disease
    • LaFerla F.M. Calcium dyshomeostasis and intracellular signalling in Alzheimer's disease. Nat. Rev. Neurosci. 3 (2002) 862-872
    • (2002) Nat. Rev. Neurosci. , vol.3 , pp. 862-872
    • LaFerla, F.M.1
  • 27
    • 3943092621 scopus 로고    scopus 로고
    • Pathways towards and away from Alzheimer's disease
    • Mattson M.P. Pathways towards and away from Alzheimer's disease. Nature 430 (2004) 631-639
    • (2004) Nature , vol.430 , pp. 631-639
    • Mattson, M.P.1
  • 28
    • 39649101710 scopus 로고    scopus 로고
    • Developing preventive therapies for chronic diseases: lessons learned from Alzheimer's disease
    • Selkoe D.J. Developing preventive therapies for chronic diseases: lessons learned from Alzheimer's disease. Nutr. Rev. 65 (2007) S239-S243
    • (2007) Nutr. Rev. , vol.65
    • Selkoe, D.J.1
  • 29
    • 67749097800 scopus 로고    scopus 로고
    • Induction of negative curvature as a mechanism of cell toxicity by amyloidogenic peptides: the case of islet amyloid polypeptide
    • Smith P., Brender J., and Ramamoorthy A. Induction of negative curvature as a mechanism of cell toxicity by amyloidogenic peptides: the case of islet amyloid polypeptide. J. Am. Chem. Soc. 131 (2009) 4470-4478
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 4470-4478
    • Smith, P.1    Brender, J.2    Ramamoorthy, A.3
  • 30
    • 34248547813 scopus 로고    scopus 로고
    • Soluble protein oligomers as emerging toxins in Alzheimer's and other amyloid diseases
    • Ferreira S.T., Vieira M.N., and De Felice F.G. Soluble protein oligomers as emerging toxins in Alzheimer's and other amyloid diseases. IUBMB Life 59 (2007) 332-345
    • (2007) IUBMB Life , vol.59 , pp. 332-345
    • Ferreira, S.T.1    Vieira, M.N.2    De Felice, F.G.3
  • 31
    • 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
    • Soong R., Brender J., Macdonald P., and Ramamoorthy A. 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.2    Macdonald, P.3    Ramamoorthy, A.4
  • 32
    • 0030892291 scopus 로고    scopus 로고
    • Characterization of the interactions of Alzheimer beta-amyloid peptides with phospholipid membranes
    • McLaurin J., and Chakrabartty A. 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
  • 33
    • 0036434382 scopus 로고    scopus 로고
    • Association of amyloid- peptide with membrane surfaces monitored by solid state NMR
    • Lindström F., Bokvist M., Sparrman T., and Gröbner G. Association of amyloid- peptide with membrane surfaces monitored by solid state NMR. Phys. Chem. Chem. Phys. 4 (2002) 5524-5530
    • (2002) Phys. Chem. Chem. Phys. , vol.4 , pp. 5524-5530
    • Lindström, F.1    Bokvist, M.2    Sparrman, T.3    Gröbner, G.4
  • 34
    • 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
    • Bokvist M., Lindstrom F., Watts A., and Grobner G. 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    Lindstrom, F.2    Watts, A.3    Grobner, G.4
  • 35
    • 34548494605 scopus 로고    scopus 로고
    • Membrane fragmentation by an amyloidogenic fragment of human islet amyloid polypeptide detected by solid-state NMR spectroscopy of membrane nanotubes
    • Brender J., Dürr U., Heyl D., Budarapu M., and Ramamoorthy A. Membrane fragmentation by an amyloidogenic fragment of human islet amyloid polypeptide detected by solid-state NMR spectroscopy of membrane nanotubes. BBA-Biomembranes 1768 (2007) 2026-2029
    • (2007) BBA-Biomembranes , vol.1768 , pp. 2026-2029
    • Brender, J.1    Dürr, U.2    Heyl, D.3    Budarapu, M.4    Ramamoorthy, A.5
  • 36
    • 0034702813 scopus 로고    scopus 로고
    • Correlation of beta-amyloid aggregate size and hydrophobicity with decreased bilayer fluidity of model membranes
    • Kremer J.J., Pallitto M.M., Sklansky D.J., and Murphy R.M. Correlation of beta-amyloid aggregate size and hydrophobicity with decreased bilayer fluidity of model membranes. Biochemistry 39 (2000) 10309-10318
    • (2000) Biochemistry , vol.39 , pp. 10309-10318
    • Kremer, J.J.1    Pallitto, M.M.2    Sklansky, D.J.3    Murphy, R.M.4
  • 37
    • 15044365726 scopus 로고    scopus 로고
    • Templating effect of lipid membranes on Alzheimer's amyloid beta peptide
    • Ege C., Majewski J., Wu G., Kjaer K., and Lee K.Y. Templating effect of lipid membranes on Alzheimer's amyloid beta peptide. Chemphyschem 6 (2005) 226-229
    • (2005) Chemphyschem , vol.6 , pp. 226-229
    • Ege, C.1    Majewski, J.2    Wu, G.3    Kjaer, K.4    Lee, K.Y.5
  • 38
    • 26944494925 scopus 로고    scopus 로고
    • Adsorption of amyloid beta (1-40) peptide at phospholipid monolayers
    • Maltseva E., Kerth A., Blume A., Mohwald H., and Brezesinski G. Adsorption of amyloid beta (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    Mohwald, H.4    Brezesinski, G.5
  • 39
    • 4444328762 scopus 로고    scopus 로고
    • Insertion of Alzheimer's A beta 40 peptide into lipid monolayers
    • Ege C., and Lee K.Y. 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.2
  • 40
    • 34547162589 scopus 로고    scopus 로고
    • Solid-state NMR as a method to reveal structure and membrane-interaction of amyloidogenic proteins and peptides
    • Naito A., and Kawamura I. Solid-state NMR as a method to reveal structure and membrane-interaction of amyloidogenic proteins and peptides. BBA-Biomembranes 1768 (2007) 1900-1912
    • (2007) BBA-Biomembranes , vol.1768 , pp. 1900-1912
    • Naito, A.1    Kawamura, I.2
  • 41
    • 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
    • Coles M., Bicknell W., Watson A., Fairlie D., and Craik D. 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    Watson, A.3    Fairlie, D.4    Craik, D.5
  • 42
    • 0033555275 scopus 로고    scopus 로고
    • Solution structures of micelle-bound amyloid beta-(1-40) and beta-(1-42) peptides of Alzheimer's disease
    • Shao H., Jao S., Ma K., and Zagorski M.G. Solution structures of micelle-bound amyloid beta-(1-40) and beta-(1-42) peptides of Alzheimer's disease. J. Mol. Biol. 285 (1999) 755-773
    • (1999) J. Mol. Biol. , vol.285 , pp. 755-773
    • Shao, H.1    Jao, S.2    Ma, K.3    Zagorski, M.G.4
  • 43
    • 34547920308 scopus 로고    scopus 로고
    • Positioning of the Alzheimer Abeta(1-40) peptide in SDS micelles using NMR and paramagnetic probes
    • Jarvet J., Danielsson J., Damberg P., Oleszczuk M., and Graslund A. Positioning of the Alzheimer Abeta(1-40) peptide in SDS micelles using NMR and paramagnetic probes. J. Biomol. NMR 39 (2007) 63-72
    • (2007) J. Biomol. NMR , vol.39 , pp. 63-72
    • Jarvet, J.1    Danielsson, J.2    Damberg, P.3    Oleszczuk, M.4    Graslund, A.5
  • 44
    • 0028335794 scopus 로고
    • Solution structure of residues 1-28 of the amyloid beta-peptide
    • Talafous J., Marcinowski K.J., Klopman G., and Zagorski M.G. Solution structure of residues 1-28 of the amyloid beta-peptide. Biochemistry 33 (1994) 7788-7796
    • (1994) Biochemistry , vol.33 , pp. 7788-7796
    • Talafous, J.1    Marcinowski, K.J.2    Klopman, G.3    Zagorski, M.G.4
  • 45
    • 0030457933 scopus 로고    scopus 로고
    • Three-dimensional structures of the amyloid beta peptide (25-35) in membrane-mimicking environment
    • Kohno T., Kobayashi K., Maeda T., Sato K., and Takashima A. Three-dimensional structures of the amyloid beta peptide (25-35) in membrane-mimicking environment. Biochemistry 35 (1996) 16094-16104
    • (1996) Biochemistry , vol.35 , pp. 16094-16104
    • Kohno, T.1    Kobayashi, K.2    Maeda, T.3    Sato, K.4    Takashima, A.5
  • 46
    • 0030983767 scopus 로고    scopus 로고
    • The interaction of beta-amyloid protein fragment (12-28) with lipid environments
    • Fletcher T.G., and Keire D.A. The interaction of beta-amyloid protein fragment (12-28) with lipid environments. Protein Sci. 6 (1997) 666-675
    • (1997) Protein Sci. , vol.6 , pp. 666-675
    • Fletcher, T.G.1    Keire, D.A.2
  • 48
    • 0028672795 scopus 로고
    • Methods to study membrane protein structure in solution
    • Henry G., and Sykes B. Methods to study membrane protein structure in solution. Methods Enzymol. 239 (1994) 515
    • (1994) Methods Enzymol. , vol.239 , pp. 515
    • Henry, G.1    Sykes, B.2
  • 49
    • 33947172767 scopus 로고    scopus 로고
    • Detergents for the stabilization and crystallization of membrane proteins
    • Privé G. Detergents for the stabilization and crystallization of membrane proteins. Methods 41 (2007) 388-397
    • (2007) Methods , vol.41 , pp. 388-397
    • Privé, G.1
  • 50
    • 33646474970 scopus 로고    scopus 로고
    • Structures of the dimeric and monomeric variants of magainin antimicrobial peptides (MSI-78 and MSI-594) in micelles and bilayers, determined by NMR spectroscopy
    • Porcelli F., Buck-Koehntop B.A., Thennarasu S., Ramamoorthy A., and Veglia G. Structures of the dimeric and monomeric variants of magainin antimicrobial peptides (MSI-78 and MSI-594) in micelles and bilayers, determined by NMR spectroscopy. Biochemistry 45 (2006) 5793-5799
    • (2006) Biochemistry , vol.45 , pp. 5793-5799
    • Porcelli, F.1    Buck-Koehntop, B.A.2    Thennarasu, S.3    Ramamoorthy, A.4    Veglia, G.5
  • 51
    • 43949083747 scopus 로고    scopus 로고
    • NMR structure of the cathelicidin-derived human antimicrobial peptide LL-37 in dodecylphosphocholine micelles
    • Porcelli F., Verardi R., Shi L., Henzler-Wildman K.A., Ramamoorthy A., and Veglia G. NMR structure of the cathelicidin-derived human antimicrobial peptide LL-37 in dodecylphosphocholine micelles. Biochemistry 47 (2008) 5565-5572
    • (2008) Biochemistry , vol.47 , pp. 5565-5572
    • Porcelli, F.1    Verardi, R.2    Shi, L.3    Henzler-Wildman, K.A.4    Ramamoorthy, A.5    Veglia, G.6
  • 52
    • 60549094781 scopus 로고    scopus 로고
    • Detergent binding explains anomalous SDS-PAGE migration of membrane proteins
    • Rath A., Glibowicka M., Nadeau V., Chen G., and Deber C. Detergent binding explains anomalous SDS-PAGE migration of membrane proteins. Proc. Natl. Acad. Sci. 106 (2009) 1760
    • (2009) Proc. Natl. Acad. Sci. , vol.106 , pp. 1760
    • Rath, A.1    Glibowicka, M.2    Nadeau, V.3    Chen, G.4    Deber, C.5
  • 54
    • 40549088246 scopus 로고    scopus 로고
    • Dimerization of the transmembrane domain of amyloid precursor proteins and familial Alzheimer's disease mutants
    • Gorman P., Kim S., Guo M., Melnyk R., McLaurin J., Fraser P., Bowie J., and Chakrabartty A. Dimerization of the transmembrane domain of amyloid precursor proteins and familial Alzheimer's disease mutants. BMC Neurosci. 9 (2008) 17
    • (2008) BMC Neurosci. , vol.9 , pp. 17
    • Gorman, P.1    Kim, S.2    Guo, M.3    Melnyk, R.4    McLaurin, J.5    Fraser, P.6    Bowie, J.7    Chakrabartty, A.8
  • 55
    • 33645504750 scopus 로고    scopus 로고
    • NMR study of the tetrameric KcsA potassium channel in detergent micelles
    • Chill J.H., Louis J.M., Miller C., and Bax A. NMR study of the tetrameric KcsA potassium channel in detergent micelles. Protein Sci. 15 (2006) 684-698
    • (2006) Protein Sci. , vol.15 , pp. 684-698
    • Chill, J.H.1    Louis, J.M.2    Miller, C.3    Bax, A.4
  • 56
    • 33746925586 scopus 로고    scopus 로고
    • Binding of amyloid beta-peptide to ganglioside micelles is dependent on histidine-13
    • Williamson M.P., Suzuki Y., Bourne N.T., and Asakura T. Binding of amyloid beta-peptide to ganglioside micelles is dependent on histidine-13. Biochem J. 397 (2006) 483-490
    • (2006) Biochem J. , vol.397 , pp. 483-490
    • Williamson, M.P.1    Suzuki, Y.2    Bourne, N.T.3    Asakura, T.4
  • 57
    • 1242269212 scopus 로고    scopus 로고
    • Alzheimer's disease: NMR studies of asialo (GM1) and trisialo (GT1b) ganglioside interactions with A (1-40) peptide in a membrane mimic environment
    • Mandal P., and Pettegrew J. Alzheimer's disease: NMR studies of asialo (GM1) and trisialo (GT1b) ganglioside interactions with A (1-40) peptide in a membrane mimic environment. Neurochem. Res. 29 (2004) 447-453
    • (2004) Neurochem. Res. , vol.29 , pp. 447-453
    • Mandal, P.1    Pettegrew, J.2
  • 58
    • 34548626252 scopus 로고    scopus 로고
    • Conformational solution studies of the SDS micelle-bound 11-28 fragment of two Alzheimer's beta-amyloid variants (E22K and A21G) using CD, NMR, and MD techniques
    • Rodziewicz-Motowidlo S., Juszczyk P., Kolodziejczyk A.S., Sikorska E., Skwierawska A., Oleszczuk M., and Grzonka Z. Conformational solution studies of the SDS micelle-bound 11-28 fragment of two Alzheimer's beta-amyloid variants (E22K and A21G) using CD, NMR, and MD techniques. Biopolymers 87 (2007) 23-39
    • (2007) Biopolymers , vol.87 , pp. 23-39
    • Rodziewicz-Motowidlo, S.1    Juszczyk, P.2    Kolodziejczyk, A.S.3    Sikorska, E.4    Skwierawska, A.5    Oleszczuk, M.6    Grzonka, Z.7
  • 61
    • 3342956450 scopus 로고    scopus 로고
    • Improvement of a critical intermediate step in the synthesis of a nitroxide-based spin-labeled deoxythymidine analog
    • Powell J., II E., and Gannett P. Improvement of a critical intermediate step in the synthesis of a nitroxide-based spin-labeled deoxythymidine analog. Molecules 5 (2000) 1244-1250
    • (2000) Molecules , vol.5 , pp. 1244-1250
    • Powell, J.1    II, E.2    Gannett, P.3
  • 62
    • 84915070406 scopus 로고
    • Nitroxyls; VII. Synthesis and reactions of highly reactive 1-oxyl-2, 2, 5, 5-tetramethyl-2, 5-dihydropyrrole-3-ylmethyl sulfonates
    • Hankovszky H., Hideg K., and Lex L. Nitroxyls; VII. Synthesis and reactions of highly reactive 1-oxyl-2, 2, 5, 5-tetramethyl-2, 5-dihydropyrrole-3-ylmethyl sulfonates. Synthesis (1980) 914-916
    • (1980) Synthesis , pp. 914-916
    • Hankovszky, H.1    Hideg, K.2    Lex, L.3
  • 63
    • 0037154097 scopus 로고    scopus 로고
    • Structure of spin-labeled methylmethanethiolsulfonate in solution and bound to TEM-1 [beta]-lactamase determined by electron nuclear double resonance spectroscopy†
    • Mustafi D., Sosa-Peinado A., Gupta V., Gordon D., and Makinen M. Structure of spin-labeled methylmethanethiolsulfonate in solution and bound to TEM-1 [beta]-lactamase determined by electron nuclear double resonance spectroscopy†. Biochemistry 41 (2002) 797-808
    • (2002) Biochemistry , vol.41 , pp. 797-808
    • Mustafi, D.1    Sosa-Peinado, A.2    Gupta, V.3    Gordon, D.4    Makinen, M.5
  • 64
    • 3142581910 scopus 로고    scopus 로고
    • Site-specific insertion of spin-labeled l-amino acids in xenopus oocytes†
    • Shafer A., Kalai T., Liu S., Hideg K., and Voss J. Site-specific insertion of spin-labeled l-amino acids in xenopus oocytes†. Biochemistry 43 (2004) 8470-8482
    • (2004) Biochemistry , vol.43 , pp. 8470-8482
    • Shafer, A.1    Kalai, T.2    Liu, S.3    Hideg, K.4    Voss, J.5
  • 66
    • 34347251258 scopus 로고    scopus 로고
    • Synthesis of TOAC spin-labeled proteins and reconstitution in lipid membranes
    • Karim C.B., Zhang Z., and Thomas D.D. Synthesis of TOAC spin-labeled proteins and reconstitution in lipid membranes. Nat. Protoc. 2 (2007) 42-49
    • (2007) Nat. Protoc. , vol.2 , pp. 42-49
    • Karim, C.B.1    Zhang, Z.2    Thomas, D.D.3
  • 67
    • 0001146033 scopus 로고    scopus 로고
    • Trifluoroacetic acid pretreatment reproducibly disaggregates the amyloid ß-peptide
    • Jao S., Ma K., Talafous J., Orlando R., and Zagorski M. Trifluoroacetic acid pretreatment reproducibly disaggregates the amyloid ß-peptide. Amyloid 4 (1997) 240-252
    • (1997) Amyloid , vol.4 , pp. 240-252
    • Jao, S.1    Ma, K.2    Talafous, J.3    Orlando, R.4    Zagorski, M.5
  • 68
    • 0032707868 scopus 로고    scopus 로고
    • Structural characterization of peptide hormone/receptor interactions by NMR spectroscopy
    • Pellegrini M., and Mierke D.F. Structural characterization of peptide hormone/receptor interactions by NMR spectroscopy. Biopolymers 51 (1999) 208-220
    • (1999) Biopolymers , vol.51 , pp. 208-220
    • Pellegrini, M.1    Mierke, D.F.2
  • 69
    • 28544450399 scopus 로고    scopus 로고
    • Biophysical and biological studies of end-group-modified derivatives of Pep-1
    • Weller K., Lauber S., Lerch M., Renaud A., Merkle H.P., and Zerbe O. Biophysical and biological studies of end-group-modified derivatives of Pep-1. Biochemistry 44 (2005) 15799-15811
    • (2005) Biochemistry , vol.44 , pp. 15799-15811
    • Weller, K.1    Lauber, S.2    Lerch, M.3    Renaud, A.4    Merkle, H.P.5    Zerbe, O.6
  • 70
    • 3242877618 scopus 로고    scopus 로고
    • DICHROWEB, an online server for protein secondary structure analyses from circular dichroism spectroscopic data
    • Whitmore L., and Wallace B. DICHROWEB, an online server for protein secondary structure analyses from circular dichroism spectroscopic data. Nucleic Acids Res. 32 (2004) W668
    • (2004) Nucleic Acids Res. , vol.32
    • Whitmore, L.1    Wallace, B.2
  • 71
    • 0027080909 scopus 로고
    • Atomic solvation parameters applied to molecular dynamics of proteins in solution
    • Wesson L., and Eisenberg D. Atomic solvation parameters applied to molecular dynamics of proteins in solution. Protein Sci. 1 (1992)
    • (1992) Protein Sci. , vol.1
    • Wesson, L.1    Eisenberg, D.2
  • 72
    • 0005963761 scopus 로고
    • Multiple quantum filters for elucidating NMR coupling networks
    • Piantini U., Sorensen O., and Ernst R. Multiple quantum filters for elucidating NMR coupling networks. J. Am. Chem. Soc. 104 (1982) 6800-6801
    • (1982) J. Am. Chem. Soc. , vol.104 , pp. 6800-6801
    • Piantini, U.1    Sorensen, O.2    Ernst, R.3
  • 73
    • 5144233105 scopus 로고
    • MLEV-17-based two-dimensional homonuclear magnetization transfer spectroscopy
    • Bax A., and Davis D. MLEV-17-based two-dimensional homonuclear magnetization transfer spectroscopy. J. Magn. Res. 65 (1985) 355-360
    • (1985) J. Magn. Res. , vol.65 , pp. 355-360
    • Bax, A.1    Davis, D.2
  • 74
    • 0343359244 scopus 로고
    • Investigation of exchange processes by two-dimensional NMR spectroscopy
    • Jeener J., Meier B., Bachmann P., and Ernst R. Investigation of exchange processes by two-dimensional NMR spectroscopy. J. Chem. Phys. 71 (1979) 4546
    • (1979) J. Chem. Phys. , vol.71 , pp. 4546
    • Jeener, J.1    Meier, B.2    Bachmann, P.3    Ernst, R.4
  • 75
    • 0004040543 scopus 로고    scopus 로고
    • University of California, San Francisco, USA
    • Goddard T., and Kneller D. SPARKY 3 software (2006), University of California, San Francisco, USA
    • (2006) SPARKY 3 software
    • Goddard, T.1    Kneller, D.2
  • 76
    • 0031576336 scopus 로고    scopus 로고
    • Torsion angle dynamics for NMR structure calculation with the new program DYANA
    • Guntert P., Mumenthaler C., and Wuthrich K. Torsion angle dynamics for NMR structure calculation with the new program DYANA. J. Mol. Biol. 273 (1997) 283-298
    • (1997) J. Mol. Biol. , vol.273 , pp. 283-298
    • Guntert, P.1    Mumenthaler, C.2    Wuthrich, K.3
  • 77
    • 0029633186 scopus 로고
    • Amber, a computer program for applying molecular mechanics, normal mode analysis, molecular dynamics and free energy calculations to elucidate the structures and energies of molecules
    • Pearlman D., Case D., Caldwell J., Ross W., Cheatham III T., DeBolt S., Ferguson D., Seibel G., and Kollman P. Amber, a computer program for applying molecular mechanics, normal mode analysis, molecular dynamics and free energy calculations to elucidate the structures and energies of molecules. Comp. Phys. Commun. 91 (1995) 1-41
    • (1995) Comp. Phys. Commun. , vol.91 , pp. 1-41
    • Pearlman, D.1    Case, D.2    Caldwell, J.3    Ross, W.4    Cheatham III, T.5    DeBolt, S.6    Ferguson, D.7    Seibel, G.8    Kollman, P.9
  • 80
    • 0026597879 scopus 로고
    • The chemical shift index: a fast and simple method for the assignment of protein secondary structure through NMR spectroscopy
    • Wishart D.S., Sykes B.D., and Richards F.M. The chemical shift index: a fast and simple method for the assignment of protein secondary structure through NMR spectroscopy. Biochemistry 31 (1992) 1647-1651
    • (1992) Biochemistry , vol.31 , pp. 1647-1651
    • Wishart, D.S.1    Sykes, B.D.2    Richards, F.M.3
  • 81
    • 0030339738 scopus 로고    scopus 로고
    • AQUA and PROCHECK-NMR: programs for checking the quality of protein structures solved by NMR
    • Laskowski R.A., Rullmannn J.A., MacArthur M.W., Kaptein R., and Thornton J.M. AQUA and PROCHECK-NMR: programs for checking the quality of protein structures solved by NMR. J. Biomol. NMR 8 (1996) 477-486
    • (1996) J. Biomol. NMR , vol.8 , pp. 477-486
    • Laskowski, R.A.1    Rullmannn, J.A.2    MacArthur, M.W.3    Kaptein, R.4    Thornton, J.M.5
  • 82
    • 0030610313 scopus 로고    scopus 로고
    • Three-dimensional structure and position of porcine motilin in sodium dodecyl sulfate micelles determined by 1H NMR†
    • Jarvet J., Zdunek J., Damberg P., and Graslund A. Three-dimensional structure and position of porcine motilin in sodium dodecyl sulfate micelles determined by 1H NMR†. Biochemistry 36 (1997) 8153-8163
    • (1997) Biochemistry , vol.36 , pp. 8153-8163
    • Jarvet, J.1    Zdunek, J.2    Damberg, P.3    Graslund, A.4
  • 83
    • 0035853015 scopus 로고    scopus 로고
    • Secondary structure and position of the cell-penetrating peptide transportan in SDS micelles as determined by NMR
    • Lindberg M., Jarvet J., Langel U., and Graslund A. Secondary structure and position of the cell-penetrating peptide transportan in SDS micelles as determined by NMR. Biochemistry 40 (2001) 3141-3149
    • (2001) Biochemistry , vol.40 , pp. 3141-3149
    • Lindberg, M.1    Jarvet, J.2    Langel, U.3    Graslund, A.4
  • 84
    • 0142249815 scopus 로고    scopus 로고
    • Micellar aggregation of alkyltrimethylammonium bromide surfactants studied by electron paramagnetic resonance of an anionic nitroxide
    • Tedeschi A., Franco L., Ruzzi M., Paduano L., Corvaja C., and D'Errico G. Micellar aggregation of alkyltrimethylammonium bromide surfactants studied by electron paramagnetic resonance of an anionic nitroxide. Phys. Chem. Chem. Phys. 5 (2003) 4204-4209
    • (2003) Phys. Chem. Chem. Phys. , vol.5 , pp. 4204-4209
    • Tedeschi, A.1    Franco, L.2    Ruzzi, M.3    Paduano, L.4    Corvaja, C.5    D'Errico, G.6
  • 85
    • 33845648492 scopus 로고    scopus 로고
    • A, Exploring interaction of beta-amyloid segment (25-35) with membrane models through paramagnetic probes
    • Esposito C., Tedeschi A., Scrima M., D'Errico G., Ottaviani M.F., Rovero P., and D'Ursi M. A, Exploring interaction of beta-amyloid segment (25-35) with membrane models through paramagnetic probes. J. Pept. Sci. 12 (2006) 766-774
    • (2006) J. Pept. Sci. , vol.12 , pp. 766-774
    • Esposito, C.1    Tedeschi, A.2    Scrima, M.3    D'Errico, G.4    Ottaviani, M.F.5    Rovero, P.6    D'Ursi, M.7
  • 86
    • 0000508196 scopus 로고
    • Theory of ESR linewidths of free radicals
    • Kivelson D. Theory of ESR linewidths of free radicals. J. Chem. Phys. 33 (1960) 1094
    • (1960) J. Chem. Phys. , vol.33 , pp. 1094
    • Kivelson, D.1
  • 87
    • 0036110838 scopus 로고    scopus 로고
    • Micellar aggregation of sulfonate surfactants studied by electron paramagnetic resonance of a cationic nitroxide: an experimental and computational approach
    • Tedeschi A., D'Errico G., Busi E., Basosi R., and Barone V. Micellar aggregation of sulfonate surfactants studied by electron paramagnetic resonance of a cationic nitroxide: an experimental and computational approach. Phys. Chem. Chem. Phys. 4 (2002) 2180-2188
    • (2002) Phys. Chem. Chem. Phys. , vol.4 , pp. 2180-2188
    • Tedeschi, A.1    D'Errico, G.2    Busi, E.3    Basosi, R.4    Barone, V.5
  • 88
    • 43249131758 scopus 로고    scopus 로고
    • Interaction of a peptide derived from glycoprotein gp36 of feline immunodeficiency virus and its lipoylated analogue with phospholipid membranes
    • D'Errico G., D'Ursi A., and Marsh D. Interaction of a peptide derived from glycoprotein gp36 of feline immunodeficiency virus and its lipoylated analogue with phospholipid membranes. Biochemistry 47 (2008) 5317
    • (2008) Biochemistry , vol.47 , pp. 5317
    • D'Errico, G.1    D'Ursi, A.2    Marsh, D.3
  • 90
    • 0036438914 scopus 로고    scopus 로고
    • Solution structure of the Alzheimer amyloid [beta]-peptide (1-42) in an apolar microenvironment: similarity with a virus fusion domain
    • Crescenzi O., Tomaselli S., Guerrini R., Salvadori S., D'Ursi A., Temussi P., and Picone D. Solution structure of the Alzheimer amyloid [beta]-peptide (1-42) in an apolar microenvironment: similarity with a virus fusion domain. Eur. J. Biochem. 269 (2002) 5642
    • (2002) Eur. J. Biochem. , vol.269 , pp. 5642
    • Crescenzi, O.1    Tomaselli, S.2    Guerrini, R.3    Salvadori, S.4    D'Ursi, A.5    Temussi, P.6    Picone, D.7
  • 92
    • 30744433878 scopus 로고    scopus 로고
    • Experimental constraints on quaternary structure in Alzheimer's beta-amyloid fibrils
    • Petkova A.T., Yau W.M., and Tycko R. Experimental constraints on quaternary structure in Alzheimer's beta-amyloid fibrils. Biochemistry 45 (2006) 498-512
    • (2006) Biochemistry , vol.45 , pp. 498-512
    • Petkova, A.T.1    Yau, W.M.2    Tycko, R.3
  • 95
    • 33751170680 scopus 로고    scopus 로고
    • Consensus features in amyloid fibrils: sheet-sheet recognition via a (polar or nonpolar) zipper structure
    • Zheng J., Ma B., and Nussinov R. Consensus features in amyloid fibrils: sheet-sheet recognition via a (polar or nonpolar) zipper structure. Phys. Biol. 3 (2006) P1-P4
    • (2006) Phys. Biol. , vol.3
    • Zheng, J.1    Ma, B.2    Nussinov, R.3


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