메뉴 건너뛰기




Volumn 4, Issue 11, 2009, Pages

RNA aptamers generated against oligomeric Aβ40 recognize common amyloid aptatopes with low specificity but high sensitivity

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID BETA PROTEIN[1-40]; AMYLOID BETA PROTEIN[1-42]; APTAMER; THIOFLAVINE; AMYLOID; AMYLOID BETA PROTEIN; LIGAND; PEPTIDE FRAGMENT; SINGLE STRANDED DNA; THIAZOLE DERIVATIVE;

EID: 70450159254     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0007694     Document Type: Article
Times cited : (63)

References (64)
  • 1
    • 65449161780 scopus 로고    scopus 로고
    • Alzheimer's disease facts and figures
    • Alzheimer's Association
    • Alzheimer's Association (2009) Alzheimer's disease facts and figures. Alzheimers Dement 5: 234-270.
    • (2009) Alzheimers Dement , vol.5 , pp. 234-270
  • 3
    • 0037426393 scopus 로고    scopus 로고
    • Visual memory predicts Alzheimer's disease more than a decade before diagnosis
    • Kawas CH, Corrada MM, Brookmeyer R, Morrison A, Resnick SM, et al. (2003) Visual memory predicts Alzheimer's disease more than a decade before diagnosis. Neurology 60: 1089-1093.
    • (2003) Neurology , vol.60 , pp. 1089-1093
    • Kawas, C.H.1    Corrada, M.M.2    Brookmeyer, R.3    Morrison, A.4    Resnick, S.M.5
  • 4
    • 3142588721 scopus 로고    scopus 로고
    • Advances in the early detection of Alzheimer's disease
    • Nestor PJ, Scheltens P, Hodges JR (2004) Advances in the early detection of Alzheimer's disease. Nat Med 10 Suppl: S34-41.
    • (2004) Nat Med , vol.10 , Issue.SUPPL.
    • Nestor, P.J.1    Scheltens, P.2    Hodges, J.R.3
  • 5
    • 33847662852 scopus 로고    scopus 로고
    • Soluble protein oligomers in neurodegeneration: Lessons from the Alzheimer's amyloid β-peptide
    • Haass C, Selkoe DJ (2007) Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer's amyloid β-peptide. Nat Rev Mol Cell Biol 8: 101-112.
    • (2007) Nat Rev Mol Cell Biol , vol.8 , pp. 101-112
    • Haass, C.1    Selkoe, D.J.2
  • 6
    • 0036708168 scopus 로고    scopus 로고
    • Paradigm shifts in Alzheimer's disease and other neurodegenerative disorders: The emerging role of oligomeric assemblies
    • Kirkitadze MD, Bitan G, Teplow DB (2002) Paradigm shifts in Alzheimer's disease and other neurodegenerative disorders: The emerging role of oligomeric assemblies. J Neurosci Res 69: 567-577.
    • (2002) J Neurosci Res , vol.69 , pp. 567-577
    • Kirkitadze, M.D.1    Bitan, G.2    Teplow, D.B.3
  • 7
    • 45249102680 scopus 로고    scopus 로고
    • Structure-function relationships of pre-fibrillar protein assemblies in Alzheimer's disease and related disorders
    • Rahimi F, Shanmugam A, Bitan G (2008) Structure-function relationships of pre-fibrillar protein assemblies in Alzheimer's disease and related disorders. Curr Alzheimer Res 5: 319-341.
    • (2008) Curr Alzheimer Res , vol.5 , pp. 319-341
    • Rahimi, F.1    Shanmugam, A.2    Bitan, G.3
  • 8
    • 33749507375 scopus 로고    scopus 로고
    • Conformation-dependent anti-amyloid oligomer antibodies
    • Kayed R, Glabe CG (2006) Conformation-dependent anti-amyloid oligomer antibodies. Methods Enzymol 413: 326-344.
    • (2006) Methods Enzymol , vol.413 , pp. 326-344
    • Kayed, R.1    Glabe, C.G.2
  • 9
    • 14044279957 scopus 로고    scopus 로고
    • Nanoparticle-based detection in cerebral spinal fluid of a soluble pathogenic biomarker for Alzheimer's disease
    • Georganopoulou DG, Chang L, Nam JM, Thaxton CS, Mufson EJ, et al. (2005) Nanoparticle-based detection in cerebral spinal fluid of a soluble pathogenic biomarker for Alzheimer's disease. Proc Natl Acad Sci USA 102: 2273-2276.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 2273-2276
    • Georganopoulou, D.G.1    Chang, L.2    Nam, J.M.3    Thaxton, C.S.4    Mufson, E.J.5
  • 10
    • 0028170719 scopus 로고
    • Soluble amyloid β-protein in the cerebrospinal fluid from patients with Alzheimer's disease, vascular dementia and controls
    • Pirttilä T, Kim KS, Mehta PD, Frey H, Wisniewski HM (1994) Soluble amyloid β-protein in the cerebrospinal fluid from patients with Alzheimer's disease, vascular dementia and controls. J Neurol Sci 127: 90-95.
    • (1994) J Neurol Sci , vol.127 , pp. 90-95
    • Pirttilä, T.1    Kim, K.S.2    Mehta, P.D.3    Frey, H.4    Wisniewski, H.M.5
  • 11
    • 58249104047 scopus 로고    scopus 로고
    • Single-domain antibodies recognize selectively small oligomeric forms of amyloid β, prevent Aβ-induced neurotoxicity and inhibit fibril formation
    • Lafaye P, Achour I, England P, Duyckaerts C, Rougeon F (2009) Single-domain antibodies recognize selectively small oligomeric forms of amyloid β, prevent Aβ-induced neurotoxicity and inhibit fibril formation. Mol Immunol 46: 695-704.
    • (2009) Mol Immunol , vol.46 , pp. 695-704
    • Lafaye, P.1    Achour, I.2    England, P.3    Duyckaerts, C.4    Rougeon, F.5
  • 12
    • 0242668337 scopus 로고    scopus 로고
    • Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis
    • Kayed R, Head E, Thompson JL, McIntire TM, Milton SC, et al. (2003) Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis. Science 300: 486-489.
    • (2003) Science , vol.300 , pp. 486-489
    • Kayed, R.1    Head, E.2    Thompson, J.L.3    McIntire, T.M.4    Milton, S.C.5
  • 13
    • 0037022297 scopus 로고    scopus 로고
    • Conformational Abs recognizing a generic amyloid fibril epitope
    • O'Nuallain B, Wetzel R (2002) Conformational Abs recognizing a generic amyloid fibril epitope. Proc Natl Acad Sci USA 99: 1485-1490.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 1485-1490
    • O'Nuallain, B.1    Wetzel, R.2
  • 14
    • 36749078121 scopus 로고    scopus 로고
    • Fibril specific, conformation dependent antibodies recognize a generic epitope common to amyloid fibrils and fibrillar oligomers that is absent in prefibrillar oligomers
    • Kayed R, Head E, Sarsoza F, Saing T, Cotman CW, et al. (2007) Fibril specific, conformation dependent antibodies recognize a generic epitope common to amyloid fibrils and fibrillar oligomers that is absent in prefibrillar oligomers. Mol Neurodegener 2: 18.
    • (2007) Mol Neurodegener , vol.2 , pp. 18
    • Kayed, R.1    Head, E.2    Sarsoza, F.3    Saing, T.4    Cotman, C.W.5
  • 16
    • 20844458090 scopus 로고    scopus 로고
    • Synaptic targeting by Alzheimer's-related amyloid β oligomers
    • Lacor PN, Buniel MC, Chang L, Fernandez SJ, Gong Y, et al. (2004) Synaptic targeting by Alzheimer's-related amyloid β oligomers. J Neurosci 24: 10191-10200.
    • (2004) J Neurosci , vol.24 , pp. 10191-10200
    • Lacor, P.N.1    Buniel, M.C.2    Chang, L.3    Fernandez, S.J.4    Gong, Y.5
  • 17
    • 33645220400 scopus 로고    scopus 로고
    • Targeting amyloid-β peptide (Aβ) oligomers by passive immunization with a conformation-selective monoclonal antibody improves learning and memory in Aβ precursor protein (APP) transgenic mice
    • Lee EB, Leng LZ, Zhang B, Kwong L, Trojanowski JQ, et al. (2006) Targeting amyloid-β peptide (Aβ) oligomers by passive immunization with a conformation-selective monoclonal antibody improves learning and memory in Aβ precursor protein (APP) transgenic mice. J Biol Chem 281: 4292-4299.
    • (2006) J Biol Chem , vol.281 , pp. 4292-4299
    • Lee, E.B.1    Leng, L.Z.2    Zhang, B.3    Kwong, L.4    Trojanowski, J.Q.5
  • 18
    • 0032860385 scopus 로고    scopus 로고
    • Aptamers: An emerging class of molecules that rival antibodies in diagnostics
    • Jayasena SD (1999) Aptamers: an emerging class of molecules that rival antibodies in diagnostics. Clin Chem 45: 1628-1650.
    • (1999) Clin Chem , vol.45 , pp. 1628-1650
    • Jayasena, S.D.1
  • 22
    • 44649202665 scopus 로고    scopus 로고
    • Application of a novel in vitro selection technique to isolate and characterise high affinity DNA aptamers binding mammalian prion proteins
    • Bibby DF, Gill AC, Kirby L, Farquhar CF, Bruce ME, et al. (2008) Application of a novel in vitro selection technique to isolate and characterise high affinity DNA aptamers binding mammalian prion proteins. J Virol Methods 151: 107-115.
    • (2008) J Virol Methods , vol.151 , pp. 107-115
    • Bibby, D.F.1    Gill, A.C.2    Kirby, L.3    Farquhar, C.F.4    Bruce, M.E.5
  • 23
    • 0141891211 scopus 로고    scopus 로고
    • Characterization of 2′-fluoro-RNA aptamers that bind preferentially to disease-associated conformations of prion protein and inhibit conversion
    • Rhie A, Kirby L, Sayer N, Wellesley R, Disterer P, et al. (2003) Characterization of 2′-fluoro-RNA aptamers that bind preferentially to disease-associated conformations of prion protein and inhibit conversion. J Biol Chem 278: 39697-39705.
    • (2003) J Biol Chem , vol.278 , pp. 39697-39705
    • Rhie, A.1    Kirby, L.2    Sayer, N.3    Wellesley, R.4    Disterer, P.5
  • 24
    • 34248598028 scopus 로고    scopus 로고
    • Thioaptamer interactions with prion proteins: Sequence-specific and non-specific binding sites
    • King DJ, Safar JG, Legname G, Prusiner SB (2007) Thioaptamer interactions with prion proteins: sequence-specific and non-specific binding sites. J Mol Biol 369: 1001-1014.
    • (2007) J Mol Biol , vol.369 , pp. 1001-1014
    • King, D.J.1    Safar, J.G.2    Legname, G.3    Prusiner, S.B.4
  • 26
    • 36348973644 scopus 로고    scopus 로고
    • Production and characterization of RNA aptamers specific for amyloid fibril epitopes
    • Bunka DH, Mantle BJ, Morten IJ, Tennent GA, Radford SE, et al. (2007) Production and characterization of RNA aptamers specific for amyloid fibril epitopes. J Biol Chem 282: 34500-34509.
    • (2007) J Biol Chem , vol.282 , pp. 34500-34509
    • Bunka, D.H.1    Mantle, B.J.2    Morten, I.J.3    Tennent, G.A.4    Radford, S.E.5
  • 27
    • 0036289319 scopus 로고    scopus 로고
    • Selection of RNA aptamers to the Alzheimer's disease amyloid peptide
    • Ylera F, Lurz R, Erdmann VA, Furste JP (2002) Selection of RNA aptamers to the Alzheimer's disease amyloid peptide. Biochem Biophys Res Commun 290: 1583-1588.
    • (2002) Biochem Biophys Res Commun , vol.290 , pp. 1583-1588
    • Ylera, F.1    Lurz, R.2    Erdmann, V.A.3    Furste, J.P.4
  • 28
    • 0035860781 scopus 로고    scopus 로고
    • Amyloid β-protein oligomerization: Prenucleation interactions revealed by photo-induced cross-linking of unmodified proteins
    • Bitan G, Lomakin A, Teplow DB (2001) Amyloid β-protein oligomerization: prenucleation interactions revealed by photo-induced cross-linking of unmodified proteins. J Biol Chem 276: 35176-35184.
    • (2001) J Biol Chem , vol.276 , pp. 35176-35184
    • Bitan, G.1    Lomakin, A.2    Teplow, D.B.3
  • 29
    • 33749518696 scopus 로고    scopus 로고
    • Structural study of metastable amyloidogenic protein oligomers by photo-induced cross-linking of unmodified proteins
    • Bitan G (2006) Structural study of metastable amyloidogenic protein oligomers by photo-induced cross-linking of unmodified proteins. Methods Enzymol 413: 217-236.
    • (2006) Methods Enzymol , vol.413 , pp. 217-236
    • Bitan, G.1
  • 30
    • 22844445895 scopus 로고    scopus 로고
    • Preparation of aggregate-free, low molecular weight amyloid-β for assembly and toxicity assays
    • Bitan G, Teplow DB (2005) Preparation of aggregate-free, low molecular weight amyloid-β for assembly and toxicity assays. Methods Mol Biol 299: 3-9.
    • (2005) Methods Mol Biol , vol.299 , pp. 3-9
    • Bitan, G.1    Teplow, D.B.2
  • 31
    • 23444445907 scopus 로고    scopus 로고
    • Competing pathways determine fibril morphology in the self-assembly of β2-microglobulin into amyloid
    • Gosal WS, Morten IJ, Hewitt EW, Smith DA, Thomson NH, et al. (2005) Competing pathways determine fibril morphology in the self-assembly of β2-microglobulin into amyloid. J Mol Biol 351: 850-864.
    • (2005) J Mol Biol , vol.351 , pp. 850-864
    • Gosal, W.S.1    Morten, I.J.2    Hewitt, E.W.3    Smith, D.A.4    Thomson, N.H.5
  • 32
    • 33144471714 scopus 로고    scopus 로고
    • A systematic study of the effect of physiological factors on β2-microglobulin amyloid formation at neutral pH
    • Myers SL, Jones S, Jahn TR, Morten IJ, Tennent GA, et al. (2006) A systematic study of the effect of physiological factors on β2-microglobulin amyloid formation at neutral pH. Biochemistry 45: 2311-2321.
    • (2006) Biochemistry , vol.45 , pp. 2311-2321
    • Myers, S.L.1    Jones, S.2    Jahn, T.R.3    Morten, I.J.4    Tennent, G.A.5
  • 33
    • 0033849738 scopus 로고    scopus 로고
    • Review: History of the amyloid fibril
    • Sipe JD, Cohen AS (2000) Review: history of the amyloid fibril. J Struct Biol 130: 88-98.
    • (2000) J Struct Biol , vol.130 , pp. 88-98
    • Sipe, J.D.1    Cohen, A.S.2
  • 34
    • 0038176528 scopus 로고    scopus 로고
    • In vitro characterization of conditions for amyloid-β peptide oligomerization and fibrillogenesis
    • Stine WB Jr, Dahlgren KN, Krafft GA, LaDu MJ (2003) In vitro characterization of conditions for amyloid-β peptide oligomerization and fibrillogenesis. J Biol Chem 278: 11612-11622.
    • (2003) J Biol Chem , vol.278 , pp. 11612-11622
    • Stine Jr, W.B.1    Dahlgren, K.N.2    Krafft, G.A.3    LaDu, M.J.4
  • 35
    • 22144462135 scopus 로고    scopus 로고
    • Neurotoxic protein oligomers - what you see is not always what you get
    • Bitan G, Fradinger EA, Spring SM, Teplow DB (2005) Neurotoxic protein oligomers - what you see is not always what you get. Amyloid 12: 88-95.
    • (2005) Amyloid , vol.12 , pp. 88-95
    • Bitan, G.1    Fradinger, E.A.2    Spring, S.M.3    Teplow, D.B.4
  • 36
    • 0032849874 scopus 로고    scopus 로고
    • Quantification of β-sheet amyloid fibril structures with thioflavin T
    • LeVine H 3rd (1999) Quantification of β-sheet amyloid fibril structures with thioflavin T. Methods Enzymol 309: 274-284.
    • (1999) Methods Enzymol , vol.309 , pp. 274-284
    • LeVine 3rd, H.1
  • 38
    • 23744463076 scopus 로고    scopus 로고
    • Pegaptanib: In exudative age-related macular degeneration
    • discussion 1578-1579
    • Siddiqui MA, Keating GM (2005) Pegaptanib: in exudative age-related macular degeneration. Drugs 65: 1571-1577; discussion 1578-1579.
    • (2005) Drugs , vol.65 , pp. 1571-1577
    • Siddiqui, M.A.1    Keating, G.M.2
  • 39
    • 32244440049 scopus 로고    scopus 로고
    • DNA aptamers that bind to PrP(C) and not PrP(Sc) show sequence and structure specificity
    • Takemura K, Wang P, Vorberg I, Surewicz W, Priola SA, et al. (2006) DNA aptamers that bind to PrP(C) and not PrP(Sc) show sequence and structure specificity. Exp Biol Med (Maywood) 231: 204-214.
    • (2006) Exp Biol Med (Maywood) , vol.231 , pp. 204-214
    • Takemura, K.1    Wang, P.2    Vorberg, I.3    Surewicz, W.4    Priola, S.A.5
  • 40
    • 35348858875 scopus 로고    scopus 로고
    • Aptamer-mediated magnetic and gold-coated magnetic nanoparticles as detection assay for prion protein assessment
    • Kouassi GK, Wang P, Sreevatan S, Irudayaraj J (2007) Aptamer-mediated magnetic and gold-coated magnetic nanoparticles as detection assay for prion protein assessment. Biotechnol Prog 23: 1239-1244.
    • (2007) Biotechnol Prog , vol.23 , pp. 1239-1244
    • Kouassi, G.K.1    Wang, P.2    Sreevatan, S.3    Irudayaraj, J.4
  • 41
    • 62449161815 scopus 로고    scopus 로고
    • Antibovine prion protein RNA aptamer containing tandem GGA repeat interacts both with recombinant bovine prion protein and its β isoform with high affinity
    • Murakami K, Nishikawa F, Noda K, Yokoyama T, Nishikawa S (2008) Antibovine prion protein RNA aptamer containing tandem GGA repeat interacts both with recombinant bovine prion protein and its β isoform with high affinity. Prion 2: 73-80.
    • (2008) Prion , vol.2 , pp. 73-80
    • Murakami, K.1    Nishikawa, F.2    Noda, K.3    Yokoyama, T.4    Nishikawa, S.5
  • 42
    • 33644958800 scopus 로고    scopus 로고
    • Amyloid formation by recombinant full-length prion proteins in phospholipid bicelle solutions
    • Lührs T, Zahn R, Wüthrich K (2006) Amyloid formation by recombinant full-length prion proteins in phospholipid bicelle solutions. J Mol Biol 357: 833-841.
    • (2006) J Mol Biol , vol.357 , pp. 833-841
    • Lührs, T.1    Zahn, R.2    Wüthrich, K.3
  • 43
    • 0037020259 scopus 로고    scopus 로고
    • Kinetic studies of amyloid β-protein fibril assembly. Differential effects of α-helix stabilization
    • Fezoui Y, Teplow DB (2002) Kinetic studies of amyloid β-protein fibril assembly. Differential effects of α-helix stabilization. J Biol Chem 277: 36948-36954.
    • (2002) J Biol Chem , vol.277 , pp. 36948-36954
    • Fezoui, Y.1    Teplow, D.B.2
  • 44
    • 0033044565 scopus 로고    scopus 로고
    • Predominance of neuronal mRNAs in individual Alzheimer's disease senile plaques
    • Ginsberg SD, Crino PB, Hemby SE, Weingarten JA, Lee VMY, et al. (1999) Predominance of neuronal mRNAs in individual Alzheimer's disease senile plaques. Ann Neurol 45: 174-181.
    • (1999) Ann Neurol , vol.45 , pp. 174-181
    • Ginsberg, S.D.1    Crino, P.B.2    Hemby, S.E.3    Weingarten, J.A.4    Lee, V.M.Y.5
  • 45
  • 46
    • 0036707495 scopus 로고    scopus 로고
    • β APP and furin mRNA concentrates in immature senile plaques in the brain of Alzheimer patients
    • Marcinkiewicz M (2002) β APP and furin mRNA concentrates in immature senile plaques in the brain of Alzheimer patients. J Neuropathol Exp Neurol 61: 815-829.
    • (2002) J Neuropathol Exp Neurol , vol.61 , pp. 815-829
    • Marcinkiewicz, M.1
  • 47
    • 0347594241 scopus 로고    scopus 로고
    • Relative influence of hydrophobicity and net charge in the aggregation of two homologous proteins
    • Calamai M, Taddei N, Stefani M, Ramponi G, Chiti F (2003) Relative influence of hydrophobicity and net charge in the aggregation of two homologous proteins. Biochemistry 42: 15078-15083.
    • (2003) Biochemistry , vol.42 , pp. 15078-15083
    • Calamai, M.1    Taddei, N.2    Stefani, M.3    Ramponi, G.4    Chiti, F.5
  • 48
    • 68049114613 scopus 로고    scopus 로고
    • Self-propagating β-sheet polypeptide structures as prebiotic informational molecular entities: The amyloid world
    • Maury CP (2009) Self-propagating β-sheet polypeptide structures as prebiotic informational molecular entities: the amyloid world. Orig Life Evol Biosph 39: 141-150.
    • (2009) Orig Life Evol Biosph , vol.39 , pp. 141-150
    • Maury, C.P.1
  • 49
    • 0030832285 scopus 로고    scopus 로고
    • In vitro selection of a 7-methyl-guanosine binding RNA that inhibits translation of capped mRNA molecules
    • Haller AA, Sarnow P (1997) In vitro selection of a 7-methyl-guanosine binding RNA that inhibits translation of capped mRNA molecules. Proc Natl Acad Sci USA 94: 8521-8526.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 8521-8526
    • Haller, A.A.1    Sarnow, P.2
  • 51
  • 52
    • 80055101575 scopus 로고    scopus 로고
    • Photo-induced cross-linking of unmodified proteins (PICUP) applied to amyloidogenic peptides
    • Rahimi F, Maiti P, Bitan G (2009) Photo-induced cross-linking of unmodified proteins (PICUP) applied to amyloidogenic peptides. J Vis Exp 23: http://www.jove.com/pubmedgen/default.aspx?PDF=&ID=1071.
    • (2009) J Vis Exp , vol.23
    • Rahimi, F.1    Maiti, P.2    Bitan, G.3
  • 53
    • 33845679081 scopus 로고    scopus 로고
    • Methods developed for SELEX
    • Gopinath SC (2007) Methods developed for SELEX. Anal Bioanal Chem 387: 171-182.
    • (2007) Anal Bioanal Chem , vol.387 , pp. 171-182
    • Gopinath, S.C.1
  • 54
    • 33645800972 scopus 로고    scopus 로고
    • RNA aptamers: From basic science towards therapy
    • Ulrich H (2006) RNA aptamers: from basic science towards therapy. Handb Exp Pharmacol. 305-326.
    • (2006) Handb Exp Pharmacol , pp. 305-326
    • Ulrich, H.1
  • 55
    • 0041923790 scopus 로고    scopus 로고
    • Inhibition of heregulin signaling by an aptamer that preferentially binds to the oligomeric form of human epidermal growth factor receptor-3
    • Chen CH, Chernis GA, Hoang VQ, Landgraf R (2003) Inhibition of heregulin signaling by an aptamer that preferentially binds to the oligomeric form of human epidermal growth factor receptor-3. Proc Natl Acad Sci USA 100: 9226-9231.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 9226-9231
    • Chen, C.H.1    Chernis, G.A.2    Hoang, V.Q.3    Landgraf, R.4
  • 56
    • 0028685490 scopus 로고
    • Fitting a mixture model by expectation maximization to discover motifs in biopolymers
    • Bailey TL, Elkan C (1994) Fitting a mixture model by expectation maximization to discover motifs in biopolymers. Proc Int Conf Intell Syst Mol Biol 2: 28-36.
    • (1994) Proc Int Conf Intell Syst Mol Biol , vol.2 , pp. 28-36
    • Bailey, T.L.1    Elkan, C.2
  • 57
    • 36448991500 scopus 로고    scopus 로고
    • Larkin MA, Blackshields G, Brown NP, Chenna R, McGettigan PA, et al, 2007 Clustal W and Clustal X version 2.0. Bioinformatics 23: 2947-2948
    • Larkin MA, Blackshields G, Brown NP, Chenna R, McGettigan PA, et al. (2007) Clustal W and Clustal X version 2.0. Bioinformatics 23: 2947-2948.
  • 58
    • 0042121256 scopus 로고    scopus 로고
    • Mfold web server for nucleic acid folding and hybridization prediction
    • Zuker M (2003) Mfold web server for nucleic acid folding and hybridization prediction. Nucleic Acids Res 31: 3406-3415.
    • (2003) Nucleic Acids Res , vol.31 , pp. 3406-3415
    • Zuker, M.1
  • 59
    • 0027480757 scopus 로고
    • The structure and mechanism of formation of human calcitonin fibrils
    • Arvinte T, Cudd A, Drake AF (1993) The structure and mechanism of formation of human calcitonin fibrils. J Biol Chem 268: 6415-6422.
    • (1993) J Biol Chem , vol.268 , pp. 6415-6422
    • Arvinte, T.1    Cudd, A.2    Drake, A.F.3
  • 60
    • 8544272519 scopus 로고    scopus 로고
    • Inhibition of islet amyloid polypeptide fibril formation: A potential role for heteroaromatic interactions
    • Porat Y, Mazor Y, Efrat S, Gazit E (2004) Inhibition of islet amyloid polypeptide fibril formation: a potential role for heteroaromatic interactions. Biochemistry 43: 14454-14462.
    • (2004) Biochemistry , vol.43 , pp. 14454-14462
    • Porat, Y.1    Mazor, Y.2    Efrat, S.3    Gazit, E.4
  • 61
    • 33646199155 scopus 로고    scopus 로고
    • Early events in insulin fibrillization studied by time-lapse atomic force microscopy
    • Podesta A, Tiana G, Milani P, Manno M (2006) Early events in insulin fibrillization studied by time-lapse atomic force microscopy. Biophys J 90: 589-597.
    • (2006) Biophys J , vol.90 , pp. 589-597
    • Podesta, A.1    Tiana, G.2    Milani, P.3    Manno, M.4
  • 62
    • 0033849915 scopus 로고    scopus 로고
    • Amyloid fibril formation and seeding by wild-type human lysozyme and its disease-related mutational variants
    • Morozova-Roche LA, Zurdo J, Spencer A, Noppe W, Receveur V, et al. (2000) Amyloid fibril formation and seeding by wild-type human lysozyme and its disease-related mutational variants. J Struct Biol 130: 339-351.
    • (2000) J Struct Biol , vol.130 , pp. 339-351
    • Morozova-Roche, L.A.1    Zurdo, J.2    Spencer, A.3    Noppe, W.4    Receveur, V.5
  • 63
    • 0027367506 scopus 로고
    • Synthetic peptides homologous to prion protein residues 106-147 form amyloid-like fibrils in vitro
    • Tagliavini F, Prelli F, Verga L, Giaccone G, Sarma R, et al. (1993) Synthetic peptides homologous to prion protein residues 106-147 form amyloid-like fibrils in vitro. Proc Natl Acad Sci USA 90: 9678-9682.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 9678-9682
    • Tagliavini, F.1    Prelli, F.2    Verga, L.3    Giaccone, G.4    Sarma, R.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.