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Volumn 50, Issue 45, 2011, Pages 9809-9816

Erratum: Distinguishing amyloid fibril structures in Alzheimer's disease (AD) by two-dimensional ultraviolet (2DUV) spectroscopy (Biochemistry (2011) 50:45 (9809-9816) DOI: 10.1021/bi201317c);Distinguishing amyloid fibril structures in Alzheimer's disease (AD) by two-dimensional ultraviolet (2DUV) spectroscopy

Author keywords

[No Author keywords available]

Indexed keywords

GLYCOPROTEINS; PROTEINS;

EID: 80755174397     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi300967d     Document Type: Erratum
Times cited : (10)

References (40)
  • 1
    • 0030799122 scopus 로고    scopus 로고
    • Amyloid β-protein fibrillogenesis: Detection of a protofibrillar intermediate
    • DOI 10.1074/jbc.272.35.22364
    • Walsh, D. M., Lomakin, A., Benedek, G. B., Condron, M. M., and Teplow, D. (1997) Amyloid β -protein fibrillogenesis: detection of a protofibrillar intermediate J. Biol. Chem. 272, 22364-22372 (Pubitemid 27382873)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.35 , pp. 22364-22372
    • Walsh, D.M.1    Lomakin, A.2    Benedek, G.B.3    Condron, M.M.4    Teplow, D.B.5
  • 2
    • 0036708168 scopus 로고    scopus 로고
    • Paradigm shifts in Alzheimer's disease and other neurodegenerative disorders: The emerging role of oligomeric assemblies
    • DOI 10.1002/jnr.10328
    • Kirkitadze, M. D., Bitan, G., and Teplow, D. B. (2002) Paradigm shifts in Alzheimer's Disease and other degenerative disorders: the emerging role of the oligomers assemblies J. Neurosci. Res. 69, 567-577 (Pubitemid 34966869)
    • (2002) Journal of Neuroscience Research , vol.69 , Issue.5 , pp. 567-577
    • Kirkitadze, M.D.1    Bitan, G.2    Teplow, D.B.3
  • 4
    • 0036438914 scopus 로고    scopus 로고
    • Solution structure of the Alzheimer amyloid β-peptide (1-42) in an apolar microenvironment: Similarity with a virus fusion domain
    • DOI 10.1046/j.1432-1033.2002.03271.x
    • Crescenzi, O., Tomaselli, S., Guerrini, R., Salvatori, S., D'Ursi, A. M., Temussi, P. A., and Picone, D. (2002) Solution structure of the Alzheimer amyloid β-peptide (1-42) in an apolar microenvironment. Similarity with a virus fusion domain Eur. J. Biochem. 269, 5642-5648 (Pubitemid 35365553)
    • (2002) European Journal of Biochemistry , vol.269 , Issue.22 , pp. 5642-5648
    • Crescenzi, O.1    Tomaselli, S.2    Guerrini, R.3    Salvadori, S.4    D'Ursi, A.M.5    Temussi, P.A.6    Picone, D.7
  • 7
    • 15944426127 scopus 로고    scopus 로고
    • Amyloid accumulation and pathogensis of Alzheimer's disease: Significance of monomeric, oligomeric and fibrillar Aβ
    • Glabe, C. G. (2005) Amyloid accumulation and pathogensis of Alzheimer's disease: significance of monomeric, oligomeric and fibrillar Aβ Subcell Biochem. 38, 167-177
    • (2005) Subcell Biochem. , vol.38 , pp. 167-177
    • Glabe, C.G.1
  • 8
    • 22444449900 scopus 로고    scopus 로고
    • On the nucleation of amyloid β-protein monomer folding
    • DOI 10.1110/ps.041292205
    • Lazo, N. D., Grant, M. A., Condron, M. C., Rigby, A. C., and Teplow, D. B. (2005) On the nucleation of amyloid β-protein monomer folding Protein Sci. 14 (6) 1581-1596 (Pubitemid 41007920)
    • (2005) Protein Science , vol.14 , Issue.6 , pp. 1581-1596
    • Lazo, N.D.1    Grant, M.A.2    Condron, M.C.3    Rigby, A.C.4    Teplow, D.B.5
  • 11
    • 33845802653 scopus 로고    scopus 로고
    • Characterizations of distinct amyloidogenic conformations of the Aβ (1-40) and (1-42) peptides
    • DOI 10.1016/j.bbrc.2006.12.043, PII S0006291X06026933
    • Lim, K. H., Collver, H. H., Le, Y. T. H., Nagchowdhuri, P., and Kenney, J. M. (2006) Characterization of distinct amyloidogenic conformations of the Aβ(1-40) and Aβ(1-42) peptides Biochem. Biophys. Res. Commun. 353, 443-449 (Pubitemid 46014583)
    • (2007) Biochemical and Biophysical Research Communications , vol.353 , Issue.2 , pp. 443-449
    • Lim, K.H.1    Collver, H.H.2    Le, Y.T.H.3    Nagchowdhuri, P.4    Kenney, J.M.5
  • 12
    • 33749535361 scopus 로고    scopus 로고
    • Preparation of Amyloid β-Protein for Structural and Functional Studies
    • DOI 10.1016/S0076-6879(06)13002-5, PII S0076687906130025, Amyloid, Prions, and Other Protein Aggregates, Part C
    • Teplow, D. B. (2006) Preparation of amyloid β-protein for structural and functional studies Methods Enzymol. 413, 20-33 (Pubitemid 44528683)
    • (2006) Methods in Enzymology , vol.413 , pp. 20-33
    • Teplow, D.B.1
  • 14
    • 67849095816 scopus 로고    scopus 로고
    • 22→G) mutation on amyloid β-protein folding: Discrete molecular dynamics study
    • 22→G) mutation on amyloid β-protein folding: discrete molecular dynamics study J. Am. Chem. Soc. 130, 17413-17422
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 17413-17422
    • Lam, A.R.1    Teplow, D.B.2    Stanley, H.E.3    Urbanc, B.4
  • 15
    • 0037135111 scopus 로고    scopus 로고
    • The amyloid hypothesis of Alzheimer's disease: Progress and problems on the road to therapeutics
    • DOI 10.1126/science.1072994
    • Hardy, J. and Selkoe, D. J. (2002) The amyloid hypothesis of Alzheimer's disease: progress and problems on the road to therapeutics Science 297, 353-356 (Pubitemid 34790756)
    • (2002) Science , vol.297 , Issue.5580 , pp. 353-356
    • Hardy, J.1    Selkoe, D.J.2
  • 16
    • 0036861112 scopus 로고    scopus 로고
    • Testing times for the "amyloid cascade hypothesis"
    • DOI 10.1016/S0197-4580(02)00042-8, PII S0197458002000428
    • Hardy, J. (2002) Testing times for the "amyloid cascade hypothesis" Neurobiol. Aging 23, 1073-1074 (Pubitemid 35447788)
    • (2002) Neurobiology of Aging , vol.23 , Issue.6 , pp. 1073-1074
    • Hardy, J.1
  • 18
    • 30744433878 scopus 로고    scopus 로고
    • Experimental constraint on quaternary structure in Alzheimer's β-amyloid fibrils
    • Petkova, A. T., Yau, W. M., and Tycko, R. (2006) Experimental constraint on quaternary structure in Alzheimer's β-amyloid fibrils Biochemistry 45, 598-512
    • (2006) Biochemistry , vol.45 , pp. 598-512
    • Petkova, A.T.1    Yau, W.M.2    Tycko, R.3
  • 19
    • 57449091884 scopus 로고    scopus 로고
    • Molecular structural basis for polymorphism in Alzheimer's β-amyloid fibrils
    • Paravastu, A., Leapman, R. D., Yau, W. M., and Tycko, R. (2008) Molecular structural basis for polymorphism in Alzheimer's β-amyloid fibrils Proc. Natl. Acad. Sci. U.S.A. 105, 18349-18354
    • (2008) Proc. Natl. Acad. Sci. U.S.A. , vol.105 , pp. 18349-18354
    • Paravastu, A.1    Leapman, R.D.2    Yau, W.M.3    Tycko, R.4
  • 20
    • 67650022104 scopus 로고    scopus 로고
    • Evidence for novel β-sheet structures in Iowa mutant β-amyloid fibrils
    • Tycko, R., Sciarretta, K. L., Orgel, J. P. R. O., and Meredith, S. C. (2009) Evidence for novel β-sheet structures in Iowa mutant β-amyloid fibrils Biochemistry 48, 6072-6084
    • (2009) Biochemistry , vol.48 , pp. 6072-6084
    • Tycko, R.1    Sciarretta, K.L.2    Orgel, J.P.R.O.3    Meredith, S.C.4
  • 21
    • 0026682931 scopus 로고
    • Solution Conformations and Aggregational Properties of Synthetic Amyloid Peptides of Alzheimer's Disease: Analysis of Circular Dichroism Spectra
    • Barrow, C. J., A., Y., Kenny, P. T. M., and Zagorski, M. G. (1992) Solution Conformations and Aggregational Properties of Synthetic Amyloid Peptides of Alzheimer's Disease: Analysis of Circular Dichroism Spectra J. Mol. Biol. 225, 1075-1093
    • (1992) J. Mol. Biol. , vol.225 , pp. 1075-1093
    • Barrow, C.J.1    A, Y.2    Kenny, P.T.M.3    Zagorski, M.G.4
  • 23
    • 36149008463 scopus 로고
    • On the transformation of light into heat in solids. i
    • Frenkel, J. (1931) On the transformation of light into heat in solids. I Phys. Rev. 37, 17-44
    • (1931) Phys. Rev. , vol.37 , pp. 17-44
    • Frenkel, J.1
  • 24
    • 0032748895 scopus 로고    scopus 로고
    • Theoretical studies toward quantitative protein circular dichroism calculations
    • Besley, N. A. and Hirst, J. D. (1999) Theoretical studies toward quantitative protein circular dichroism calculations J. Am. Chem. Soc. 121, 9636-9644
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 9636-9644
    • Besley, N.A.1    Hirst, J.D.2
  • 25
    • 17644386516 scopus 로고    scopus 로고
    • The exciton model and the circular dichroism of polypeptides
    • DOI 10.1007/s00706-004-0279-2
    • Woody, R. W. (2005) The exciton model and the circular dichroism of polypeptides Monatsh. Chem. 136, 347-366 (Pubitemid 40562073)
    • (2005) Monatshefte fur Chemie , vol.136 , Issue.3 , pp. 347-366
    • Woody, R.W.1
  • 27
    • 67649261996 scopus 로고    scopus 로고
    • Coherent multidimensional optical spectroscopy of excitons in molecular aggregates; Quasiparticle versus supermolecule perspectives
    • Abramavicius, D., Palmieri, B., Voronine, D. V., Sanda, F., and Mukamel, S. (2009) Coherent multidimensional optical spectroscopy of excitons in molecular aggregates; quasiparticle versus supermolecule perspectives Chem. Rev. 109, 2350-2408
    • (2009) Chem. Rev. , vol.109 , pp. 2350-2408
    • Abramavicius, D.1    Palmieri, B.2    Voronine, D.V.3    Sanda, F.4    Mukamel, S.5
  • 28
    • 33847696560 scopus 로고    scopus 로고
    • Amide i two-dimensional infrared spectroscopy of β-hairpin peptides
    • Smith, A. W. and Tokmakoff, A. (2007) Amide I two-dimensional infrared spectroscopy of β-hairpin peptides J. Chem. Phys. 125, 045109-1-10
    • (2007) J. Chem. Phys. , vol.125 , pp. 04510901-04510910
    • Smith, A.W.1    Tokmakoff, A.2
  • 30
    • 44349183090 scopus 로고    scopus 로고
    • Tracking fiber formation in human islet amyloid polypeptide with automated 2D-IR spectroscopy
    • DOI 10.1021/ja801483n
    • Strasfeld, D. B., Ling, Y. L., Shim, S.-H., and Zanni, M. T. (2008) Tracking fiber formation in human islet amyloid polypeptide with automated 2D-IR spectroscopy J. Am. Chem. Soc. 130, 6698-6699 (Pubitemid 351748393)
    • (2008) Journal of the American Chemical Society , vol.130 , Issue.21 , pp. 6698-6699
    • Strasfeld, D.B.1    Ling, Y.L.2    Shim, S.-H.3    Zanni, M.T.4
  • 31
    • 66149084447 scopus 로고    scopus 로고
    • Two-dimensional IR spectroscopy and isotope labeling defines the pathway of amyloid formation with residue-specific resolution
    • Shim, S.-H., Gupta, R., Ling, Y. L., Strasfeld, D. B., Raleigh, D. P., and Zanni, M. T. (2009) Two-dimensional IR spectroscopy and isotope labeling defines the pathway of amyloid formation with residue-specific resolution Proc. Natl. Acad. Sci. U.S.A. 106, 6614-6619
    • (2009) Proc. Natl. Acad. Sci. U.S.A. , vol.106 , pp. 6614-6619
    • Shim, S.-H.1    Gupta, R.2    Ling, Y.L.3    Strasfeld, D.B.4    Raleigh, D.P.5    Zanni, M.T.6
  • 32
    • 77956622554 scopus 로고    scopus 로고
    • Ultraviolet spectroscopy of protein backbone transitions in aqueous solution: Combined QM and MM simulations
    • Jiang, J., Abramavicius, D., Bulheller, B. M., Hirst, J. D., and Mukamel, S. (2010) Ultraviolet spectroscopy of protein backbone transitions in aqueous solution: combined QM and MM simulations J. Phys. Chem. B 114, 8270-8277
    • (2010) J. Phys. Chem. B , vol.114 , pp. 8270-8277
    • Jiang, J.1    Abramavicius, D.2    Bulheller, B.M.3    Hirst, J.D.4    Mukamel, S.5
  • 33
    • 78650154823 scopus 로고    scopus 로고
    • Two-dimensional ultraviolet (2DUV) spectroscopic tools for identifying fibrillation propensity of protein residue sequences
    • Jiang, J. and Mukamel, S. (2010) Two-dimensional ultraviolet (2DUV) spectroscopic tools for identifying fibrillation propensity of protein residue sequences Angew. Chem. 49, 9666-9669
    • (2010) Angew. Chem. , vol.49 , pp. 9666-9669
    • Jiang, J.1    Mukamel, S.2
  • 34
    • 79251591658 scopus 로고    scopus 로고
    • Two-dimensional near-ultraviolet spectroscopy of aromatic residues in amyloid fibrils: A first principles study
    • Jiang, J. and Mukamel, S. (2011) Two-dimensional near-ultraviolet spectroscopy of aromatic residues in amyloid fibrils: a first principles study Phys. Chem. Chem. Phys. 13, 2394-2400
    • (2011) Phys. Chem. Chem. Phys. , vol.13 , pp. 2394-2400
    • Jiang, J.1    Mukamel, S.2
  • 36
    • 0041784950 scopus 로고    scopus 로고
    • All-atom empirical potential for molecular modeling and dynamics studies of proteins
    • MacKerell, A. D. 1998, All-atom empirical potential for molecular modeling and dynamics studies of proteins J. Comput. Chem. 102, 3586-3616
    • (1998) J. Comput. Chem. , vol.102 , pp. 3586-3616
    • MacKerell, A.D.1
  • 39
    • 79956106725 scopus 로고    scopus 로고
    • Probing amyloid fibril growth by two-dimensional near-ultraviolet spectroscopy
    • Jiang, J. and Mukamel, S. (2011) Probing amyloid fibril growth by two-dimensional near-ultraviolet spectroscopy J. Phys. Chem. B 115, 6321-6328
    • (2011) J. Phys. Chem. B , vol.115 , pp. 6321-6328
    • Jiang, J.1    Mukamel, S.2
  • 40
    • 0031983456 scopus 로고    scopus 로고
    • Pathologic amyloid β-protein cell surface fibril assembly on cultured human cerebrovascular smooth muscle cells
    • Van Nostrand, W. E., Melchor, J. P., and Ruffini, L. (1998) Pathologic amyloid β-protein cell surface fibril assembly on cultured human cerebrovascular smooth muscle cells J. Neurochem. 70, 216-223 (Pubitemid 28020846)
    • (1998) Journal of Neurochemistry , vol.70 , Issue.1 , pp. 216-223
    • Van Nostrand, W.E.1    Melchor, J.P.2    Ruffini, L.3


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