메뉴 건너뛰기




Volumn 59, Issue 2, 2012, Pages 307-312

Nature of cross-seeding barriers of amyloidogenesis

Author keywords

Amyloidogenesis; Amyloids; Cross seeding; Cross species barriers; Prion; PrP23 144

Indexed keywords

ANIMALIA; BOVINAE; CERVIDAE;

EID: 84867150758     PISSN: 0001527X     EISSN: 1734154X     Source Type: Journal    
DOI: 10.18388/abp.2012_2156     Document Type: Article
Times cited : (1)

References (33)
  • 1
    • 79953183597 scopus 로고    scopus 로고
    • Atomic structures suggest determinants of transmission barriers in mammalian prion disease
    • Apostol MI, Wiltzius JJ, Sawaya MR, Cascio D, Eisenberg D (2011) Atomic structures suggest determinants of transmission barriers in mammalian prion disease. Biochemistry 50: 2456-2463.
    • (2011) Biochemistry , vol.50 , pp. 2456-2463
    • Apostol, M.I.1    Wiltzius, J.J.2    Sawaya, M.R.3    Cascio, D.4    Eisenberg, D.5
  • 2
    • 57049093241 scopus 로고    scopus 로고
    • Amyloidogenesis in its biological environment: challenging a fundamental issue in protein misfolding diseases
    • Bellotti V, Chiti F (2008) Amyloidogenesis in its biological environment: challenging a fundamental issue in protein misfolding diseases. Curr Opin Struct Biol 18: 771-779.
    • (2008) Curr Opin Struct Biol , vol.18 , pp. 771-779
    • Bellotti, V.1    Chiti, F.2
  • 3
    • 80052813251 scopus 로고    scopus 로고
    • Sequence specificity and fidelity of prion transmission in yeast
    • Bruce KL, Chernoff YO (2011) Sequence specificity and fidelity of prion transmission in yeast. Sem Cell Dev Biol 22: 444-451.
    • (2011) Sem Cell Dev Biol , vol.22 , pp. 444-451
    • Bruce K.L.Chernoff, Y.O.1
  • 4
    • 33847307713 scopus 로고    scopus 로고
    • Prion species barrier between the closely related yeast proteins is detected despite coaggregation
    • Chen B, Newnam GP Chernoff YO (2007) Prion species barrier between the closely related yeast proteins is detected despite coaggregation. Proc Natl Acad Sci USA 104: 2791-2796.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 2791-2796
    • Chen, B.1    Newnam, G.P.2    Chernoff, Y.O.3
  • 5
    • 33746377894 scopus 로고    scopus 로고
    • Protein misfolding, functional amyloid, and human disease
    • Chiti F, Dobson CM (2006) Protein misfolding, functional amyloid, and human disease. Annu Rev Biochem 75: 333-366.
    • (2006) Annu Rev Biochem , vol.75 , pp. 333-366
    • Chiti, F.1    Dobson, C.M.2
  • 6
    • 0037155826 scopus 로고    scopus 로고
    • A designed system for assessing how sequence affects alpha to beta conformational transitions in proteins
    • Ciani B, Hutchinson EG, Sessions RB, Woolfson DN (2002) A designed system for assessing how sequence affects alpha to beta conformational transitions in proteins. J Biol Chem 277: 10150-10155.
    • (2002) J Biol Chem , vol.277 , pp. 10150-10155
    • Ciani, B.1    Hutchinson, E.G.2    Sessions, R.B.3    Woolfson, D.N.4
  • 7
    • 58049199406 scopus 로고    scopus 로고
    • Prion protein amyloid formation under native-like conditions involves refolding of the Cterminal alpha-helical domain
    • Cobb NJ, Apetri AC, Surewicz WK (2008) Prion protein amyloid formation under native-like conditions involves refolding of the Cterminal alpha-helical domain. Proc Natl Acad Sci USA 283: 34704-34711.
    • (2008) Proc Natl Acad Sci USA , vol.283 , pp. 34704-34711
    • Cobb, N.J.1    Apetri, A.C.2    Surewicz, W.K.3
  • 9
    • 28044457195 scopus 로고    scopus 로고
    • The amyloid stretch hypothesis: recruiting proteins toward the dark side
    • Esteras-Chopo A, Serrano L, López de la Paz M (2005) The amyloid stretch hypothesis: recruiting proteins toward the dark side. Proc Natl Acad Sci USA 102: 16672-16677.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 16672-16677
    • Esteras-Chopo, A.1    Serrano, L.2    López de la Paz, M.3
  • 11
    • 0017873321 scopus 로고
    • Analysis of the accuracy and implications of simple methods for predicting the secondary structure of globular proteins
    • Garnier J, Osguthorpe DJ, Robson B (1978) Analysis of the accuracy and implications of simple methods for predicting the secondary structure of globular proteins. J Mol Biol 120: 97-120.
    • (1978) J Mol Biol , vol.120 , pp. 97-120
    • Garnier, J.1    Osguthorpe, D.J.2    Robson, B.3
  • 12
    • 0029884694 scopus 로고    scopus 로고
    • GOR secondary structure prediction method version IV
    • Garnier J, Gibrat J-F, Robson B (1996) GOR secondary structure prediction method version IV. Methods Enzymol 266: 540-553.
    • (1996) Methods Enzymol , vol.266 , pp. 540-553
    • Garnier, J.1    Gibrat, J.-F.2    Robson, B.3
  • 13
    • 33644940173 scopus 로고    scopus 로고
    • Mutagenesis of the central hydrophobic cluster in Abeta42 Alzheimer's peptide. Side-chain properties correlate with aggregation propensities
    • de Groot NS, Aviles FX, Vendrell J, Ventura S ( 2006) Mutagenesis of the central hydrophobic cluster in Abeta42 Alzheimer's peptide. Side-chain properties correlate with aggregation propensities. FEBS J 273: 658-668.
    • (2006) FEBS J , vol.273 , pp. 658-668
    • de Groot, N.S.1    Aviles, F.X.2    Vendrell, J.3    Ventura, S.4
  • 14
    • 22044455269 scopus 로고    scopus 로고
    • A toy model for predicting the rate of amyloid formation from unfolded protein
    • Hall D, Hirota N, Dobson CM (2005) A toy model for predicting the rate of amyloid formation from unfolded protein. J Mol Biol 351: 195-205.
    • (2005) J Mol Biol , vol.351 , pp. 195-205
    • Hall, D.1    Hirota, N.2    Dobson, C.M.3
  • 15
    • 80052320137 scopus 로고    scopus 로고
    • Intermolecular alignment in Y145Stop human prion protein amyloid fibrils probed by solid-state NMR spectroscopy
    • Helmus JJ, Surewicz K, Apostol MI, Surewicz WK, Jaroniec CP (2011) Intermolecular alignment in Y145Stop human prion protein amyloid fibrils probed by solid-state NMR spectroscopy. J Am Chem Soc 133: 13934-13937.
    • (2011) J Am Chem Soc , vol.133 , pp. 13934-11937
    • Helmus, J.J.1    Surewicz, K.2    Apostol, M.I.3    Surewicz, W.K.4    Jaroniec, C.P.5
  • 16
    • 34047157022 scopus 로고    scopus 로고
    • Hydrophobic cooperativity as a mechanism for amyloid nucleation
    • Hills RD Jr, Brooks CL. 3rd. (2007) Hydrophobic cooperativity as a mechanism for amyloid nucleation. J Mol Biol 368: 894-901.
    • (2007) J Mol Biol , vol.368 , pp. 894-901
    • Hills Jr., R.D.1    Brooks III, C.L.2
  • 17
    • 17044381327 scopus 로고    scopus 로고
    • Fibril conformation as the basis of species- and strain-dependent seeding specificity of mammalian prion amyloids
    • Jones EM, Surewicz WK (2005) Fibril conformation as the basis of species- and strain-dependent seeding specificity of mammalian prion amyloids. Cell 121: 63-72.
    • (2005) Cell , vol.121 , pp. 63-72
    • Jones, E.M.1    Surewicz, W.K.2
  • 19
    • 33750430630 scopus 로고    scopus 로고
    • Generic hydrophobic residues are sufficient to promote aggregation of the Alzheimer's Abeta42 peptide
    • Kim W, Hecht MH (2006) Generic hydrophobic residues are sufficient to promote aggregation of the Alzheimer's Abeta42 peptide. Proc Natl Acad Sci USA 103: 15824-15829.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 15824-15829
    • Kim, W.1    Hecht, M.H.2
  • 20
    • 40049110948 scopus 로고    scopus 로고
    • Mutations Enhance the Aggregation Propensity of the Alzheimer's Abeta Peptide
    • Kim W, Hecht MH (2008) Mutations Enhance the Aggregation Propensity of the Alzheimer's Abeta Peptide. J Mol Biol 377: 565-574.
    • (2008) J Mol Biol , vol.377 , pp. 565-574
    • Kim, W.1    Hecht, M.H.2
  • 21
    • 0142091396 scopus 로고    scopus 로고
    • Nucleation-dependent conformational conversion of the Y145Stop variant of human prion protein: structural clues for prion propagation
    • Kundu B, Maiti NR, Jones EM, Surewicz KA, Vanik DL, Surewicz WK (2003) Nucleation-dependent conformational conversion of the Y145Stop variant of human prion protein: structural clues for prion propagation. Proc Natl Acad Sci USA 100: 12069-12074.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 12074-12074
    • Kundu, B.1    Maiti, N.R.2    Jones, E.M.3    Surewicz, K.A.4    Vanik, D.L.5    Surewicz, W.K.6
  • 22
    • 0020475449 scopus 로고
    • A simple method for displaying the hydropathic character of a protein
    • Kyte J, Doolittle RF (1982) A simple method for displaying the hydropathic character of a protein. J Mol Biol 157: 105-132.
    • (1982) J Mol Biol , vol.157 , pp. 105-132
    • Kyte, J.1    Doolittle, R.F.2
  • 23
    • 33846811599 scopus 로고    scopus 로고
    • Beta-sheet core of human prion protein amyloid fibrils as determined by hydrogen/deuterium exchange
    • Lu X, Wintrode PL, Surewicz WK (2007). Beta-sheet core of human prion protein amyloid fibrils as determined by hydrogen/deuterium exchange. Proc Natl Acad Sci USA 104: 1510-1515.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 1510-1515
    • Lu, X.1    Wintrode, P.L.2    Surewicz, W.K.3
  • 24
    • 57649128935 scopus 로고    scopus 로고
    • Fibrils with parallel in-register structure constitute a major class of amyloid fibrils: molecular insights from electron paramagnetic resonance spectroscopy
    • Margittai M, Langen R (2008) Fibrils with parallel in-register structure constitute a major class of amyloid fibrils: molecular insights from electron paramagnetic resonance spectroscopy. Q Rev Biophys 41: 265-297.
    • (2008) Q Rev Biophys , vol.41 , pp. 265-297
    • Margittai, M.1    Langen, R.2
  • 25
    • 78650164509 scopus 로고    scopus 로고
    • Molecular interactions between prions as seeds and recombinant prion proteins as substrates resemble the biological interspecies barrier in vitro
    • Panza G, Luers L, Stohr J, Nagel-Steger L, Weiss J, Riesner D, Willbold D, Birkmann E (2010) Molecular interactions between prions as seeds and recombinant prion proteins as substrates resemble the biological interspecies barrier in vitro. PLOS One 5: e14283.
    • (2010) PLOS One , vol.5
    • Panza, G.1    Luers, L.2    Stohr, J.3    Nagel-Steger, L.4    Weiss, J.5    Riesner, D.6    Willbold, D.7    Birkmann, E.8
  • 26
    • 0020321767 scopus 로고
    • Novel proteinaceous infectious particles cause scrapie
    • Prusiner SB (1982) Novel proteinaceous infectious particles cause scrapie. Science 216: 136-144.
    • (1982) Science , vol.216 , pp. 136-144
    • Prusiner, S.B.1
  • 27
    • 17444393233 scopus 로고    scopus 로고
    • Higher-order molecular packing in amyloid-like fibrils constructed with linear arrangements of hydrophobic and hydrogen-bonding side-chains
    • Saiki M, Honda S, Kawasaki K, Zhou D, Kaito A, Konakahara T, Mori H (2005) Higher-order molecular packing in amyloid-like fibrils constructed with linear arrangements of hydrophobic and hydrogen-bonding side-chains. J Mol Biol 348: 983-998.
    • (2005) J Mol Biol , vol.348 , pp. 983-998
    • Saiki, M.1    Honda, S.2    Kawasaki, K.3    Zhou, D.4    Kaito, A.5    Konakahara, T.6    Mori, H.7
  • 28
    • 78751675430 scopus 로고    scopus 로고
    • Probing aromatic, hydrophobic, and steric effects on the self-assembly of an amyloid-ß fragment peptide
    • Senguen FT, Lee NR, Gu X, Ryan DM, Doran TM, Anderson EA, Nilsson BL (2011a) Probing aromatic, hydrophobic, and steric effects on the self-assembly of an amyloid-ß fragment peptide. Mol Biosyst 7: 486-496.
    • (2011) Mol Biosyst , vol.7 , pp. 486-496
    • Senguen, F.T.1    Lee, N.R.2    Gu, X.3    Ryan, D.M.4    Doran, T.M.5    Anderson, E.A.6    Nilsson, B.L.7
  • 29
    • 78751674190 scopus 로고    scopus 로고
    • Clarifying the influence of core amino acid hydrophobicity, secondary structure propensity, and molecular volume on amyloid-β 16-22 self-assembly
    • Senguen FT, Doran TM, Anderson EA, Nilsson BL (2011b) Clarifying the influence of core amino acid hydrophobicity, secondary structure propensity, and molecular volume on amyloid-β 16-22 self-assembly. Mol Biosyst 7: 497-510.
    • (2011) Mol Biosyst , vol.7 , pp. 497-510
    • Senguen, F.T.1    Doran, T.M.2    Anderson, E.A.3    Nilsson, B.L.4
  • 30
    • 33749822624 scopus 로고    scopus 로고
    • The emerging principles of mammalian prion propagation and transmissibility barriers: Insight from studies in vitro
    • Surewicz WK, Jones EM, Apetri AC (2006). The emerging principles of mammalian prion propagation and transmissibility barriers: Insight from studies in vitro. Acc Chem Res 39: 654-662.
    • (2006) Acc Chem Res , vol.39 , pp. 654-662
    • Surewicz, W.K.1    Jones, E.M.2    Apetri, A.C.3
  • 31
    • 25844466604 scopus 로고    scopus 로고
    • Prediction of aggregation rate and aggregation-prone segments in polypeptide sequences
    • Tartaglia GG, Cavalli A, Pellarin R, Caflisch A (2005) Prediction of aggregation rate and aggregation-prone segments in polypeptide sequences. Protein Sci 14: 2723-2734.
    • (2005) Protein Sci , vol.14 , pp. 2723-2734
    • Tartaglia, G.G.1    Cavalli, A.2    Pellarin, R.3    Caflisch, A.4
  • 33
    • 1842766124 scopus 로고    scopus 로고
    • Molecular basis of barriers for interspecies transmissibility of mammalian prions
    • Vanik DL, Surewicz KA, Surewicz WK (2004) Molecular basis of barriers for interspecies transmissibility of mammalian prions. Mol Cell 14: 139-145.
    • (2004) Mol Cell , vol.14 , pp. 139-145
    • Vanik, D.L.1    Surewicz, K.A.2    Surewicz, W.K.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.