Amyloid fibrillogenesis: themes and variations

被引：964
作者：
Rochet, JC [1 ]
Lansbury, PT [1 ]
机构：
[1] Harvard Univ, Sch Med, Brigham & Womens Hosp, Dept Neurol,Ctr Neurol Dis, Boston, MA 02115 USA
来源：
CURRENT OPINION IN STRUCTURAL BIOLOGY | 2000年 / 10卷 / 01期
关键词：
D O I：
10.1016/S0959-440X(99)00049-4
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
Recent progress has improved our knowledge of how proteins form amyloid fibrils. Both 'natively unfolded' and globular proteins have been shown to initiate fibrillization by adopting a partially structured conformation. Oligomeric prefibrillar intermediates have been extensively characterized with respect to their morphology and temporal evolution. Three-dimensional models obtained using biophysical and computational methods have provided information about fibril structure. All of these advances suggest common features of self-assembly pathways, with subtle variations accounting for differences among distinct amyloid fibrils.
引用
收藏
页码：60 / 68
页数：9
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共 77 条
  • [1] An NMR investigation of solution aggregation reactions preceding the misassembly of acid-denatured cold shock protein A into fibrils
    Alexandrescu, AT
    Rathgeb-Szabo, K
    [J]. JOURNAL OF MOLECULAR BIOLOGY, 1999, 291 (05) : 1191 - 1206
  • [2] Propagating structure of Alzheimer's β-amyloid(10-35) is parallel β-sheet with residues in exact register
    Benzinger, TLS
    Gregory, DM
    Burkoth, TS
    Miller-Auer, H
    Lynn, DG
    Botto, RE
    Meredith, SC
    [J]. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1998, 95 (23) : 13407 - 13412
  • [3] Morphological development of β(1-40) amyloid fibrils
    Blackley, HKL
    Patel, N
    Davies, MC
    Roberts, CJ
    Tendler, SJB
    Wilkinson, MJ
    Williams, PM
    [J]. EXPERIMENTAL NEUROLOGY, 1999, 158 (02) : 437 - 443
  • [4] Synchrotron X-ray studies suggest that the core of the transthyretin amyloid fibril is a continuous beta-sheet helix
    Blake, C
    Serpell, L
    [J]. STRUCTURE, 1996, 4 (08) : 989 - 998
  • [5] Mechanistic studies of the folding of human lysozyme and the origin of amyloidogenic behavior in its disease-related variants
    Canet, D
    Sunde, M
    Last, AM
    Miranker, A
    Spencer, A
    Robinson, CV
    Dobson, CM
    [J]. BIOCHEMISTRY, 1999, 38 (20) : 6419 - 6427
  • [6] Biophysical characterization of lithostathine - Evidences for a polymeric structure at physiological, pH and a proteolysis mechanism leading to the formation of fibrils
    Cerini, C
    Peyrot, V
    Garnier, C
    Duplan, L
    Veesler, S
    Le Caer, JP
    Bernard, JP
    Bouteille, H
    Michel, R
    Vazi, A
    Dupuy, P
    Michel, B
    Berland, Y
    Verdier, JM
    [J]. JOURNAL OF BIOLOGICAL CHEMISTRY, 1999, 274 (32) : 22266 - 22274
  • [7] Designing conditions for in vitro formation of amyloid protofilaments and fibrils
    Chiti, F
    Webster, P
    Taddei, N
    Clark, A
    Stefani, M
    Ramponi, G
    Dobson, CM
    [J]. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1999, 96 (07) : 3590 - 3594
  • [8] Islet amyloid polypeptide: Actions and role in the pathogenesis of diabetes
    Clark, A
    Charge, SBP
    Badman, MK
    MacArthur, DA
    deKoning, EJP
    [J]. BIOCHEMICAL SOCIETY TRANSACTIONS, 1996, 24 (02) : 594 - 599
  • [9] Acceleration of oligomerization, not fibrillization, is a shared property of both α-synuclein mutations linked to early-onset Parkinson's disease:: Implications for pathogenesis and therapy
    Conway, KA
    Lee, SJ
    Rochet, JC
    Ding, TT
    Williamson, RE
    Lansbury, PT
    [J]. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2000, 97 (02) : 571 - 576
  • [10] Accelerated in vitro fibril formation by a mutant α-synuclein linked to early-onset Parkinson disease
    Conway, KA
    Harper, JD
    Lansbury, PT
    [J]. NATURE MEDICINE, 1998, 4 (11) : 1318 - 1320
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