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Volumn 6, Issue 5, 2011, Pages

Amyloid-associated nucleic acid hybridisation

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID PROTEIN; NUCLEIC ACID; AMYLOID; AMYLOID BETA PROTEIN; AMYLOID PRECURSOR PROTEIN; APP PROTEIN, HUMAN; PEPTIDE NUCLEIC ACID;

EID: 79956266642     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0019125     Document Type: Article
Times cited : (33)

References (44)
  • 1
    • 71549169557 scopus 로고    scopus 로고
    • Neurodegeneration. Could they all be prion diseases?
    • Miller G, (2009) Neurodegeneration. Could they all be prion diseases? Science 326: 1337-1339.
    • (2009) Science , vol.326 , pp. 1337-1339
    • Miller, G.1
  • 3
    • 0036845354 scopus 로고    scopus 로고
    • The behaviour of polyamino acids reveals an inverse side chain effect in amyloid structure formation
    • Fandrich M, Dobson CM, (2002) The behaviour of polyamino acids reveals an inverse side chain effect in amyloid structure formation. Embo J 21: 5682-5690.
    • (2002) Embo J , vol.21 , pp. 5682-5690
    • Fandrich, M.1    Dobson, C.M.2
  • 4
    • 0035826234 scopus 로고    scopus 로고
    • Amyloid fibrils from muscle myoglobin
    • Fandrich M, Fletcher MA, Dobson CM, (2001) Amyloid fibrils from muscle myoglobin. Nature 410: 165-166.
    • (2001) Nature , vol.410 , pp. 165-166
    • Fandrich, M.1    Fletcher, M.A.2    Dobson, C.M.3
  • 7
    • 34249290108 scopus 로고    scopus 로고
    • Atomic structures of amyloid cross-[bgr] spines reveal varied steric zippers
    • Sawaya MR, Sambashivan S, Nelson R, Ivanova MI, Sievers SA, et al. (2007) Atomic structures of amyloid cross-[bgr] spines reveal varied steric zippers. Nature 447: 453-457.
    • (2007) Nature , vol.447 , pp. 453-457
    • Sawaya, M.R.1    Sambashivan, S.2    Nelson, R.3    Ivanova, M.I.4    Sievers, S.A.5
  • 8
    • 0037022563 scopus 로고    scopus 로고
    • Natural beta-sheet proteins use negative design to avoid edge-to-edge aggregation
    • Richardson JS, Richardson DC, (2002) Natural beta-sheet proteins use negative design to avoid edge-to-edge aggregation. Proc Natl Acad Sci U S A 99: 2754-2759.
    • (2002) Proc Natl Acad Sci U S A , vol.99 , pp. 2754-2759
    • Richardson, J.S.1    Richardson, D.C.2
  • 9
    • 0037022661 scopus 로고    scopus 로고
    • Rationally designed mutations convert de novo amyloid-like fibrils into monomeric beta-sheet proteins
    • Wang W, Hecht MH, (2002) Rationally designed mutations convert de novo amyloid-like fibrils into monomeric beta-sheet proteins. Proc Natl Acad Sci U S A 99: 2760-2765.
    • (2002) Proc Natl Acad Sci U S A , vol.99 , pp. 2760-2765
    • Wang, W.1    Hecht, M.H.2
  • 12
    • 33745224979 scopus 로고    scopus 로고
    • Collagen plays an active role in the aggregation of beta2-microglobulin under physiopathological conditions of dialysis-related amyloidosis
    • Relini A, Canale C, De Stefano S, Rolandi R, Giorgetti S, et al. (2006) Collagen plays an active role in the aggregation of beta2-microglobulin under physiopathological conditions of dialysis-related amyloidosis. J Biol Chem 281: 16521-16529.
    • (2006) J Biol Chem , vol.281 , pp. 16521-16529
    • Relini, A.1    Canale, C.2    de Stefano, S.3    Rolandi, R.4    Giorgetti, S.5
  • 13
    • 8544264563 scopus 로고    scopus 로고
    • Double-stranded DNA stimulates the fibrillation of alpha-synuclein in vitro and is associated with the mature fibrils: an electron microscopy study
    • Cherny D, Hoyer W, Subramaniam V, Jovin TM, (2004) Double-stranded DNA stimulates the fibrillation of alpha-synuclein in vitro and is associated with the mature fibrils: an electron microscopy study. J Mol Biol 344: 929-938.
    • (2004) J Mol Biol , vol.344 , pp. 929-938
    • Cherny, D.1    Hoyer, W.2    Subramaniam, V.3    Jovin, T.M.4
  • 14
    • 0142184333 scopus 로고    scopus 로고
    • RNA molecules stimulate prion protein conversion
    • Deleault NR, Lucassen RW, Supattapone S, (2003) RNA molecules stimulate prion protein conversion. Nature 425: 717-720.
    • (2003) Nature , vol.425 , pp. 717-720
    • Deleault, N.R.1    Lucassen, R.W.2    Supattapone, S.3
  • 16
    • 7944223439 scopus 로고    scopus 로고
    • Nucleic Acid and Prion Protein Interaction Produces Spherical Amyloids which can Function in vivo as Coats of Spongiform Encephalopathy Agent
    • Nandi PK, Nicole JC, (2004) Nucleic Acid and Prion Protein Interaction Produces Spherical Amyloids which can Function in vivo as Coats of Spongiform Encephalopathy Agent. J Mol Biol 344: 827-837.
    • (2004) J Mol Biol , vol.344 , pp. 827-837
    • Nandi, P.K.1    Nicole, J.C.2
  • 17
    • 33750353368 scopus 로고    scopus 로고
    • Nature and significance of the interactions between amyloid fibrils and biological polyelectrolytes
    • Calamai M, Kumita JR, Mifsud J, Parrini C, Ramazzotti M, et al. (2006) Nature and significance of the interactions between amyloid fibrils and biological polyelectrolytes. Biochemistry 45: 12806-12815.
    • (2006) Biochemistry , vol.45 , pp. 12806-12815
    • Calamai, M.1    Kumita, J.R.2    Mifsud, J.3    Parrini, C.4    Ramazzotti, M.5
  • 19
    • 77649213673 scopus 로고    scopus 로고
    • Generating a prion with bacterially expressed recombinant prion protein
    • Wang F, Wang X, Yuan CG, Ma J, (2010) Generating a prion with bacterially expressed recombinant prion protein. Science 327: 1132-1135.
    • (2010) Science , vol.327 , pp. 1132-1135
    • Wang, F.1    Wang, X.2    Yuan, C.G.3    Ma, J.4
  • 21
    • 0035127031 scopus 로고    scopus 로고
    • A domain-swapped RNase A dimer with implications for amyloid formation
    • Liu Y, Gotte G, Libonati M, Eisenberg D, (2001) A domain-swapped RNase A dimer with implications for amyloid formation. Nat Struct Mol Biol 8: 211-214.
    • (2001) Nat Struct Mol Biol , vol.8 , pp. 211-214
    • Liu, Y.1    Gotte, G.2    Libonati, M.3    Eisenberg, D.4
  • 22
    • 0025077964 scopus 로고
    • Chemical activity of simple basic peptides
    • Brack A, Barbier B, (1990) Chemical activity of simple basic peptides. Orig Life Evol Biosph 20: 139-144.
    • (1990) Orig Life Evol Biosph , vol.20 , pp. 139-144
    • Brack, A.1    Barbier, B.2
  • 23
    • 3343003514 scopus 로고    scopus 로고
    • Techniques to study amyloid fibril formation in vitro
    • Nilsson MR, (2004) Techniques to study amyloid fibril formation in vitro. Methods 34: 151-160.
    • (2004) Methods , vol.34 , pp. 151-160
    • Nilsson, M.R.1
  • 24
    • 0031825554 scopus 로고    scopus 로고
    • From the globular to the fibrous state: protein structure and structural conversion in amyloid formation
    • Sunde M, Blake CC, (1998) From the globular to the fibrous state: protein structure and structural conversion in amyloid formation. Q Rev Biophys 31: 1-39.
    • (1998) Q Rev Biophys , vol.31 , pp. 1-39
    • Sunde, M.1    Blake, C.C.2
  • 25
    • 0027452496 scopus 로고
    • A study of oligonucleotide reassociation using large arrays of oligonucleotides synthesised on a glass support
    • Maskos U, Southern EM, (1993) A study of oligonucleotide reassociation using large arrays of oligonucleotides synthesised on a glass support. Nucleic Acids Res 21: 4663-4669.
    • (1993) Nucleic Acids Res , vol.21 , pp. 4663-4669
    • Maskos, U.1    Southern, E.M.2
  • 26
    • 0028881098 scopus 로고
    • The biophysics of DNA hybridization with immobilized oligonucleotide probes
    • Chan V, Graves DJ, McKenzie SE, (1995) The biophysics of DNA hybridization with immobilized oligonucleotide probes. Biophys J 69: 2243-2255.
    • (1995) Biophys J , vol.69 , pp. 2243-2255
    • Chan, V.1    Graves, D.J.2    McKenzie, S.E.3
  • 27
    • 41149089304 scopus 로고    scopus 로고
    • Poly(L-lysine)-graft-dextran copolymer accelerates DNA hybridisation by two orders
    • Wu L, Shimada N, Kano A, Maruyama A, (2008) Poly(L-lysine)-graft-dextran copolymer accelerates DNA hybridisation by two orders. Soft Matter 4: 744-747.
    • (2008) Soft Matter , vol.4 , pp. 744-747
    • Wu, L.1    Shimada, N.2    Kano, A.3    Maruyama, A.4
  • 29
    • 0041473475 scopus 로고    scopus 로고
    • Cations as mediators of the adsorption of nucleic acids on clay surfaces in prebiotic environments
    • Franchi M, Ferris JP, Gallori E, (2003) Cations as mediators of the adsorption of nucleic acids on clay surfaces in prebiotic environments. Orig Life Evol Biosph 33: 1-16.
    • (2003) Orig Life Evol Biosph , vol.33 , pp. 1-16
    • Franchi, M.1    Ferris, J.P.2    Gallori, E.3
  • 30
    • 33646265028 scopus 로고    scopus 로고
    • Protein and nucleic acid together: A mechanism for the emergence of biological selection
    • Dale T, (2006) Protein and nucleic acid together: A mechanism for the emergence of biological selection. J Theor Biol 240: 337-342.
    • (2006) J Theor Biol , vol.240 , pp. 337-342
    • Dale, T.1
  • 31
    • 0032584573 scopus 로고    scopus 로고
    • Peptides by activation of amino acids with CO on (Ni,Fe)S surfaces: implications for the origin of life
    • Huber C, Wachtershauser G, (1998) Peptides by activation of amino acids with CO on (Ni,Fe)S surfaces: implications for the origin of life. Science 281: 670-672.
    • (1998) Science , vol.281 , pp. 670-672
    • Huber, C.1    Wachtershauser, G.2
  • 32
    • 66149108671 scopus 로고    scopus 로고
    • Synthesis of activated pyrimidine ribonucleotides in prebiotically plausible conditions
    • Powner MW, Gerland B, Sutherland JD, (2009) Synthesis of activated pyrimidine ribonucleotides in prebiotically plausible conditions. Nature 459: 239-242.
    • (2009) Nature , vol.459 , pp. 239-242
    • Powner, M.W.1    Gerland, B.2    Sutherland, J.D.3
  • 33
    • 78349253629 scopus 로고    scopus 로고
    • Polyphosphate-peptide synergy and the organic takeover at the emergence of life
    • Milner-White EJ, Russell MJ, (2010) Polyphosphate-peptide synergy and the organic takeover at the emergence of life. Journal of Cosmology 10: 3217-3229.
    • (2010) Journal of Cosmology , vol.10 , pp. 3217-3229
    • Milner-White, E.J.1    Russell, M.J.2
  • 35
    • 48349105059 scopus 로고    scopus 로고
    • Novel dual inhibitory function aptamer-siRNA delivery system for HIV-1 therapy
    • Zhou J, Li H, Li S, Zaia J, Rossi JJ, (2008) Novel dual inhibitory function aptamer-siRNA delivery system for HIV-1 therapy. Mol Ther 16: 1481-1489.
    • (2008) Mol Ther , vol.16 , pp. 1481-1489
    • Zhou, J.1    Li, H.2    Li, S.3    Zaia, J.4    Rossi, J.J.5
  • 36
    • 0032532357 scopus 로고    scopus 로고
    • Secondary structure analysis of the putative membrane-associated domains of the inward rectifier K+ channel ROMK1
    • Brazier SP, Ramesh B, Haris PI, Lee DC, Srai SK, (1998) Secondary structure analysis of the putative membrane-associated domains of the inward rectifier K+ channel ROMK1. Biochem J 335 (Pt 2): 375-380.
    • (1998) Biochem J , vol.335 , Issue.Pt 2 , pp. 375-380
    • Brazier, S.P.1    Ramesh, B.2    Haris, P.I.3    Lee, D.C.4    Srai, S.K.5
  • 37
    • 0033576275 scopus 로고    scopus 로고
    • Fourier transform infrared spectroscopic studies of the interaction of the antimicrobial peptide gramicidin S with lipid micelles and with lipid monolayer and bilayer membranes
    • Lewis RN, Prenner EJ, Kondejewski LH, Flach CR, Mendelsohn R, et al. (1999) Fourier transform infrared spectroscopic studies of the interaction of the antimicrobial peptide gramicidin S with lipid micelles and with lipid monolayer and bilayer membranes. Biochemistry 38: 15193-15203.
    • (1999) Biochemistry , vol.38 , pp. 15193-15203
    • Lewis, R.N.1    Prenner, E.J.2    Kondejewski, L.H.3    Flach, C.R.4    Mendelsohn, R.5
  • 38
    • 0037663875 scopus 로고    scopus 로고
    • Bethesda, US National Institutes of Health
    • Rasband WS, (1997) Image J Bethesda US National Institutes of Health.
    • (1997) Image J
    • Rasband, W.S.1
  • 39
  • 40
    • 79956278613 scopus 로고    scopus 로고
    • X-Ray Diffraction Studies of Amyloid Structure
    • Amyloid Proteins: Methods and Protocols: Springer
    • Makin OS, Serpell CS, (2002) X-Ray Diffraction Studies of Amyloid Structure. pp. 67-80 Amyloid Proteins: Methods and Protocols: Springer.
    • (2002) , pp. 67-80
    • Makin, O.S.1    Serpell, C.S.2
  • 43
    • 20544435097 scopus 로고    scopus 로고
    • Exploring the helix-coil transition via all-atom equilibrium ensemble simulations
    • Sorin EJ, Pande VS, (2005) Exploring the helix-coil transition via all-atom equilibrium ensemble simulations. Biophys J 88: 2472-2493.
    • (2005) Biophys J , vol.88 , pp. 2472-2493
    • Sorin, E.J.1    Pande, V.S.2


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