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Volumn 18, Issue 4, 2007, Pages

Analysis of structural order in amyloid fibrils

Author keywords

[No Author keywords available]

Indexed keywords

AGGLOMERATION; ATOMIC FORCE MICROSCOPY; CONFORMATIONS; DENSITY (SPECIFIC GRAVITY); METABOLISM; MOLECULAR STRUCTURE; SUPRAMOLECULAR CHEMISTRY;

EID: 33846818885     PISSN: 09574484     EISSN: 13616528     Source Type: Journal    
DOI: 10.1088/0957-4484/18/4/044031     Document Type: Article
Times cited : (10)

References (28)
  • 1
    • 0347357617 scopus 로고    scopus 로고
    • Protein folding and misfolding
    • Dobson C M 2003 Protein folding and misfolding Nature 426 884-90
    • (2003) Nature , vol.426 , Issue.6968 , pp. 884-890
    • Dobson, C.M.1
  • 2
    • 0346727128 scopus 로고    scopus 로고
    • Therapeutic approaches to protein-misfolding diseases
    • Cohen F E and Kelly J W 2003 Therapeutic approaches to protein-misfolding diseases Nature 426 905-9
    • (2003) Nature , vol.426 , Issue.6968 , pp. 905-909
    • Cohen, F.E.1    Kelly, J.W.2
  • 3
    • 0035961329 scopus 로고    scopus 로고
    • The structural basis of protein folding and its links with human disease
    • Dobson C M 2001 The structural basis of protein folding and its links with human disease Phil. Trans. R. Soc. B 356 133-45
    • (2001) Phil. Trans. R. Soc. , vol.356 , Issue.1406 , pp. 133-145
    • Dobson, C.M.1
  • 5
    • 33748481341 scopus 로고    scopus 로고
    • X-ray scattering study of the effect of hydration on the cross-beta structure of amyloid fibrils
    • Squires A M, Devlin G L, Gras S L, Tickler A K, MacPhee C E and Dobson C M 2006 X-ray scattering study of the effect of hydration on the cross-beta structure of amyloid fibrils J. Am. Chem. Soc. 128 11738-9
    • (2006) J. Am. Chem. Soc. , vol.128 , Issue.36 , pp. 11738-11739
    • Squires, A.M.1    Devlin, G.L.2    Gras, S.L.3    Tickler, A.K.4    MacPhee, C.E.5    Dobson, C.M.6
  • 9
    • 0042847751 scopus 로고    scopus 로고
    • Cryo-electron microscopy structure of an SH3 amyloid fibril and model of the molecular packing
    • Jimenez J L, Guijarro J I, Orlova E, Zurdo J, Dobson C M, Sunde M and Saibil H R 1999 Cryo-electron microscopy structure of an SH3 amyloid fibril and model of the molecular packing EMBO J. 18 815-21
    • (1999) EMBO J. , vol.18 , Issue.4 , pp. 815-821
    • Jimenez, J.L.1    Guijarro, J.I.2    Orlova, E.3    Zurdo, J.4    Dobson, C.M.5    Sunde, M.6    Saibil, H.R.7
  • 11
    • 0032570543 scopus 로고    scopus 로고
    • Folding kinetics of the SH3 domain of PI3 kinase by real-time nmr combined with optical spectroscopy
    • Guijarro J I, Morton C J, Plaxco K W, Campbell I D and Dobson C M 1998 Folding kinetics of the SH3 domain of PI3 kinase by real-time nmr combined with optical spectroscopy J. Mol. Biol. 276 657-67
    • (1998) J. Mol. Biol. , vol.276 , Issue.3 , pp. 657-667
    • Guijarro, J.I.1    Morton, C.J.2    Plaxco, K.W.3    Campbell, I.D.4    Dobson, C.M.5
  • 13
    • 0031444010 scopus 로고    scopus 로고
    • Atomic force microscopic imaging of seeded fibril formation and fibril branching by the alzheimer's disease amyloid-beta protein
    • Harper J D, Lieber C M and Lansbury P T 1997 Atomic force microscopic imaging of seeded fibril formation and fibril branching by the alzheimer's disease amyloid-beta protein Chem. Biol. 4 951-9
    • (1997) Chem. Biol. , vol.4 , Issue.12 , pp. 951-959
    • Harper, J.D.1    Lieber, C.M.2    Lansbury, P.T.3
  • 15
    • 2342522638 scopus 로고    scopus 로고
    • Understanding the diversity of prions
    • Aguzzi A 2004 Understanding the diversity of prions Nat. Cell. Biol. 6 290-2
    • (2004) Nat. Cell. Biol. , vol.6 , Issue.4 , pp. 290-292
    • Aguzzi, A.1
  • 16
    • 33746698975 scopus 로고    scopus 로고
    • The physical basis of how prion conformations determine strain phenotypes
    • Tanaka M, Collins S R, Toyama B H and Weissman J S 2006 The physical basis of how prion conformations determine strain phenotypes Nature 442 585-9
    • (2006) Nature , vol.442 , Issue.7102 , pp. 585-589
    • Tanaka, M.1    Collins, S.R.2    Toyama, B.H.3    Weissman, J.S.4
  • 17
    • 17044381327 scopus 로고    scopus 로고
    • Fibril conformation as the basis of species-and strain-dependent seeding specificity of mammalian prion amyloids
    • Jones E M and Surewicz W K 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 , Issue.1 , pp. 63-72
    • Jones, E.M.1    Surewicz, W.K.2
  • 18
    • 12244249201 scopus 로고    scopus 로고
    • Self-propagating, molecular-level polymorphism in alzheimer's beta-amyloid fibrils
    • Petkova A T, Leapman R D, Guo Z, Yau W, Mattson M P and Tycko R 2005 Self-propagating, molecular-level polymorphism in alzheimer's beta-amyloid fibrils Science 307 262-5
    • (2005) Science , vol.307 , Issue.5707 , pp. 262-265
    • Petkova, A.T.1    Leapman, R.D.2    Guo, Z.3    Yau, W.4    Mattson, M.P.5    Tycko, R.6
  • 19
    • 33744831968 scopus 로고    scopus 로고
    • Polymorphic fibril formation by residues 10-40 of the alzheimer's beta-amyloid peptide
    • Paravastu A K, Petkova A T and Tycko R 2006 Polymorphic fibril formation by residues 10-40 of the alzheimer's beta-amyloid peptide Biophys. J. 90 4618-29
    • (2006) Biophys. J. , vol.90 , Issue.12 , pp. 4618-4629
    • Paravastu, A.K.1    Petkova, A.T.2    Tycko, R.3
  • 21
    • 0002932259 scopus 로고
    • Bemerkungen über umwandlungstemperaturen
    • Peierls R E 1934 Bemerkungen über umwandlungstemperaturen Helv. Phys. Acta Suppl. 7 81
    • (1934) Helv. Phys. Acta Suppl. , vol.7 , pp. 81
    • Peierls, R.E.1
  • 26
    • 0033777523 scopus 로고    scopus 로고
    • Formation of insulin amyloid fibrils followed by ftir simultaneously with cd and electron microscopy
    • Bouchard M, Zurdo J, Nettleton E J, Dobson C M and Robinson C V 2000 Formation of insulin amyloid fibrils followed by ftir simultaneously with cd and electron microscopy Protein Sci. 9 1960-7
    • (2000) Protein Sci. , vol.9 , pp. 1960-1967
    • Bouchard, M.1    Zurdo, J.2    Nettleton, E.J.3    Dobson, C.M.4    Robinson, C.V.5
  • 27
    • 18844387881 scopus 로고    scopus 로고
    • A cylinder-shaped double ribbon structure formed by an amyloid hairpin peptide derived from the beta-sheet of murine prp: An x-ray and molecular dynamics simulation study
    • Croixmarie V, Briki F, David G, Coc Y, Ovtracht L, Doucet J, Jamin N and Sanson A 2005 A cylinder-shaped double ribbon structure formed by an amyloid hairpin peptide derived from the beta-sheet of murine prp: an x-ray and molecular dynamics simulation study J. Struct. Biol. 150 284-99
    • (2005) J. Struct. Biol. , vol.150 , Issue.3 , pp. 284-299
    • Croixmarie, V.1    Briki, F.2    David, G.3    Coc, Y.4    Ovtracht, L.5    Doucet, J.6    Jamin, N.7    Sanson, A.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.